ライフサイエンスコーパス: pore domain

1 R is located in the highly conserved channel pore domain.

2 s across the plasma membrane via a conserved pore domain.

3 athways, because Hv1 channels lack a classic pore domain.

4 -loop does not form a complete, transferable pore domain.

5 ) to form the voltage-sensing domain and the pore domain.

6 vents strong nonannular lipid binding to the pore domain.

7 e between the voltage-sensing domain and the pore domain.

8 r subunit consists of a voltage sensor and a pore domain.

9 eing the voltage-sensor domain and S5-S6 the pore domain.

10 for activation of the VSD and opening of the pore domain.

11 ation require interaction with the channel's pore domain.

12 rchitecture, containing a VSD, but lacking a pore domain.

13 ers composed of four voltage sensors and one pore domain.

14 molecular dynamics simulations of the Kv1.2 pore domain.

15 code a voltage sensor domain (VSD) without a pore domain.

16 a voltage-sensor domain, lacking a separate pore domain.

17 This study concerns the pore domain.

18 e VSD that functions as both the VSD and the pore domain.

19 discovered that contain a single VSD but no pore domain.

20 ains (VSDs) that surround the K(+) selective pore domain.

21 ing between the extracellular domain and the pore domain.

22 nker that connects the voltage sensor to the pore domain.

23 modeled after the crystal structure of KvAP pore domain.

24 critical amino acid residues located in the pore domain.

25 r ends of the voltage-sensor domains and the pore domain.

26 part describes molecular modeling of hERG's pore domain.

27 termining whether S4 packs against S5 of the pore domain.

28 ic question as to whether S4 is close to the pore domain.

29 connect the nucleotide binding pocket to the pore domain.

30 eration of the slow inactivation gate in the pore domain.

31 interface of VSD(II) and the tightly closed pore domain.

32 hen the interface between voltage sensor and pore domain.

33 r, rather than the hydrophobic cavity of the pore domain.

34 between the cytoplasmic RCK domains and the pore domain.

35 e, indicating an allosteric influence of the pore domain.

36 nts to control ionic conductance through the pore domain.

37 with a conserved Trp residue in the channel pore domain.

38 s or mass transfer coefficients in different pore domains.

39 communication between the ligand-binding and pore domains.

40 ansition zone between the ligand-binding and pore domains.

41 family of background K(+) channels with two pore domains.

42 ol one ion permeation pathway formed by four pore domains.

43 uctural link between the voltage sensing and pore domains.

44 ct interface between the voltage-sensing and pore domains.

45 uggested an interaction between neighbouring pore domains.

46 oton channels, both of which lack associated pore domains.

47 or non-swapped arrangements of the S1-S4 and pore domains.

48 at functionally links the ligand binding and pore domains.

49 embrane (S1-S6) proteins that form a central pore domain (4 x S5-S6) surrounded by four voltage senso

50 s activated by low pH and the other is the 2-pore domain acid-sensing K(+) channel (TASK1), which is

51 sed of four subunits, and each subunit has a pore domain and a voltage-sensing domain (VSD).

52 K(v) channel by systematically mutating the pore domain and assessing tolerance by examining channel

53 pathways or "side portals" that separate the pore domain and associated cytosolic structures covering

54 ains (VSDs) that regulate the opening of the pore domain and ensuing permeation of sodium ions.

55 Voltage-gated K+ channels contain a central pore domain and four surrounding voltage-sensing domains

56 single amino acids identified Thr-312 of the pore domain and Ile-337, Phe-339, Phe-340, and Ala-344 o

57 phore attached at one of 37 positions in the pore domain and in the S4 voltage sensor of the Shaker K

58 ructural rearrangements include the putative pore domain and reveal the location of an intracellular

59 in establishing functional contacts between pore domain and the cellular membrane.

60 models and giving a higher resolution of the pore domain and the structural transitions it undergoes

61 lent link between the voltage sensor and the pore domain and used this information as restraints for

62 dicates that Tyr-542 interacts with both the pore domain and voltage sensor residues to stabilize act

63 s at a cleft between the voltage-sensing and pore domains and appears to affect the channel gate by a

64 tage sensing S4, the pore loop and S6 in the pore domain, and intracellular calmodulin-binding helix

65 Inwardly rectifying, voltage-gated, two-pore domain, and related K(+) channels are located in eu

66 mperature and voltage sensor modules and the pore domain, and then discuss the thermodynamic foundati

67 the VSD at its peripheral junction with the pore domain, and then plunge into the core of the VSD in

68 ng of transmembrane (TM) voltage-sensing and pore domains, and a cytoplasmic carboxy-terminal domain.

69 transduction between the gating ring and the pore domain appears to be enhanced.

70 ric Torpedo nicotinic acetylcholine receptor pore domain are also described.

71 hey also find that its interactions with the pore domain are rather complex, with specific S4-S5 inte

72 sly uncharacterized function for the channel-pore domain as a regulator of channel trafficking.

73 he interface between the voltage-sensing and pore domain as crucial for inverted electromechanical co

74 onformational changes of a potassium channel pore domain as it progresses along its gating cycle.

75 The four pore domains assemble to form one single central pore, a

76 low gating, but mutations in the cytoplasmic pore domain at E224 and E299 have been shown to induce f

77 Calciseptine sits on the shoulder of the pore domain, away from the permeation path.

78 TREK-1 is a two-pore domain background K+ channel (KCNK2, K2P2.1) that i

79 that can fold and function as the channel's pore domain between E2172 and the last residue E2547.

80 VSD protein (H(V)1) that lacks a discernible pore domain but is sufficient for expression of a voltag

81 imply attributable to a stabilization of the pore domain but that S4 undergoes conformational changes

82 ow a protein that contains only a VSD and no pore domain can conduct ions.

83 ies have shown that lidocaine binding to the pore domain causes a decrease in the maximum gating (Qma

84 We identify the two-pore domain channel THIK-1 as the main K(+) channel expr

85 TASK-1 and TASK-3, members of the two-pore-domain channel family, are widely expressed leak po

86 rane domains and, unlike other cloned tandem pore domain channels, a PDZ (postsynaptic density protei

87 This pore-domain chimera is permeable to Na(+), K(+), and Ca(

88 consequence of nonconserved residues in both pore domains contributing to the selectivity filter (T11

89 well as reducing the voltage sensing domain-pore domain coupling and shifting the zero voltage equil

90 oltage sensor, which interacts with a closed pore domain directly via two interfaces and indirectly v

91 verapamil traverse the central cavity of the pore domain, directly blocking ion permeation.

92 arate pore domain, or, in channels lacking a pore domain, directly gates an ion pathway within the VS

93 omain couples chemical ligand binding to the pore domain during channel gating.

94 Internal pore domains exist within rocks, lithic fragments, subsu

95 Potassium channels in the two-pore domain family (K2P) have various structural attribu

96 Strikingly, in the pore domain, flipping of a M3 residue within a conserved

97 of four homologous domains (DI-DIV), with a pore domain formed by the S5 and S6 segments and a volta

98 both the voltage-sensor-like domain and the pore domain, forming a gating ring that couples conforma

99 cts that S4 is located in the groove between pore domains from different subunits, rather than at the

100 d at the interface between membrane-spanning pore domains from each of four subunits, and the gates o

101 Asn in both S6s result in uncoupling of the pore domains from their voltage-sensor domains.

102 ain (VSD), the Ca(2+)-binding sites, and the pore domain govern the mammalian Ca(2+)- and voltage-act

103 TM alpha-helices, we found that TM1, a Cx26 pore domain, had a strong propensity to homodimerize.

104 The tandem pore domain halothane-inhibited K(+) channel 1 (THIK1) p

105 tracellular loops extending from the channel pore domains has been referred to as a transmission inte

106 subsequent tilting motion of the S4s and the pore domain helices, S5s, of all four subunits induces a

107 ate the physical distance between S4 and the pore domain in functional channels in a native membrane

108 eas the more versatile SM interacts with the pore domain in repeat I of Na(v)s.

109 voltage-sensor domains operate on a central pore domain in response to membrane voltage.

110 hich the S4 voltage sensor packs against the pore domain in the hyperpolarized, or "down," state of S

111 (+) channel that has served as the archetype pore domain in the Kv channel superfamily.

112 ve investigated how S4 moves relative to the pore domain in the prototypical Shaker potassium channel

113 tion, and S4 lies in close apposition to the pore domain in the resting and activated state.

114 utagenesis on the transmembrane shell of the pore domain in the Shaker voltage-gated K+ channel to lo

115 The structure reveals a pore domain in which the pore-lining S6 helix connects t

116 K2P K(+) channels with two pore domains in tandem associate as dimers to produce so

117 ing coupling between the voltage-sensing and pore domains in tetrameric voltage-gated channels.

118 es targeting cardiac TREK-1 (TWIK [tandem of pore-domains in a weakly inward rectifying potassium cha

119 muli sensors are allosterically coupled to a pore domain, increasing the probability of finding the c

120 terminal membrane pore; the insertion of the pore domain into the bacterial outer membrane follows th

121 sition of M1 and M2 in the upper part of the pore domain is likely to remain constant during the ASIC

122 The pore domain is missing in Hv1.

123 hannel's voltage-sensing domain, whereas the pore domain is nonfunctional.

124 The Piezo1 pore domain is not pressure-sensitive and the appending

125 opening, tight association of the S1-S4 and pore domains is stabilized by changes in the carboxy-ter

126 P6-S, as a membrane protein extrinsic to the pore domain, is necessary and sufficient to explain a fu

127 We demonstrate that by exchanging the pore domains JYL-1421, which is modality-selective in ra

128 endent K channels (Kv4, Kv7, and Kv11), twin-pore domain K channels (TASK, TREK), inward rectifier Ki

129 selectivity filter (SF), including many two-pore domain K(+) (K(2P)) channels, voltage-gated hERG (h

130 are neuronally expressed members of the two-pore domain K(+) (K2P) channel family and are mechanosen

131 transduction in TRAAK and TREK1 (K2P2.1) two-pore domain K(+) (K2P) channels come from the lipid memb

132 Two-pore domain K(+) (K2P) channels have many important phys

133 TRAAK channels, members of the two-pore domain K(+) (potassium ion) channel family K2P, are

134 pporting significant contribution of the two-pore domain K(+) channel (K(2P)) isoforms, TWIK-1 and TR

135 vestigated TASK channels, members of the two-pore domain K(+) channel family, as a component of the K

136 TREK-1, a two-pore domain K(+) channel, was the first animal mechanose

137 ted K(+) channel (TREK-1) belongs to the two-pore domain K(+) channels (K2P) and displays various pro

138 Two-pore domain K(+) channels (K2P) mediate background K(+)

139 ional pharmacological screening regimen, two-pore domain K(+) channels (K2P) were identified as the K

140 TWIK-1 two-pore domain K(+) channels generally produce nonmeasurabl

141 (<5% O2), in addition to inhibiting the two-pore domain K(+) channels TASK-1/3 (TASK), indirectly ac

142 ay and accounts for the insensitivity of two-pore domain K(+) channels to inhibitory toxins.

143 ediated via activating TREK-2, a type of two-pore domain K(+) channels, and required the functions of

144 of TASK-3 (KCNK9) channels, a subtype of two-pore domain K(+) channels, mimicked the SF effects by in

145 EC by activating the TWIK-1 type of the two-pore domain K(+) channels.

146 TREK-2 (K2P10.1), a member of the two-pore domain K+ (K2P) channel family, provides the backgr

147 Two-pore domain K+ (K2P) channels play an important role in

148 We show that TASK-1, a two pore domain K+ channel, provides a prominent leak K+ cur

149 The acid-sensitive, two-pore domain K+ channel, TASK-1, contributes to the backg

150 udy, we provide strong evidence that the two-pore domain K+ channel, TASK-1, mediates a noninactivati

151 Tandem pore domain K+ channels represent a new family of ion ch

152 ockers, suggesting that TRH inhibits the two-pore domain K+ channels.

153 d compared with those of recently cloned two pore domain K+ channels.

154 reviously reported the expression of the two-pore-domain K channel TREK-1 in lung epithelial cells an

155 annel (TRAAK) form the TREK subfamily of two-pore-domain K(+) (K2P) channels.

156 the rat and mouse of mRNA encoding seven two-pore-domain K(+) channel family members: TASK-1 (KCNK3),

157 arly counterbalance hypokalaemia-induced two pore-domain K(+) channel isoform 1 (K2P1) leak cation cu

158 ardiomyocytes with ectopic expression of two pore-domain K(+) channel isoform 1 (K2P1) recapitulate t

159 EK channels belong to the superfamily of two-pore-domain K(+) channels and are activated by membrane

160 Two-pore-domain K(+) channels provide neuronal background cu

161 nnel-related acid-sensitive K+ channel-1]) 2-pore-domain K+ (K(2P)) channels have been implicated in

162 produce a dominant negative for TRESK, a two-pore-domain K+ channel implicated in migraine: TRESK-MT,

163 t, with properties characteristic of the two-pore-domain K+ channel TASK-1.

164 m currents carried by the KCNK family of two-pore-domain K+ channels are important determinants of re

165 This review discusses the role of 2-pore-domain K+ channels in contributing to background co

166 As mRNA for the two-pore-domain K+ channels TASK-1 (KCNK3) and TASK-3 (KCNK9

167 The recently described two-pore-domain K+ channels, TASK-1 and TASK-3, generate cur

168 and inhibits TREK1 and TREK2, two other two-pore-domain K+ channels, to increase trigeminal sensory

169 TREK-1 is a two-pore domain (K(2P)) potassium channel that carries a lea

170 ls, including pharmacologically relevant two-pore domain (K2P) and big potassium (BK) channels.

171 SK1 is a member of the K(+)-selective tandem-pore domain (K2P) channel family.

172 Recent X-ray crystal structures of the two-pore domain (K2P) family of potassium channels have reve

173 TREK-2 is a mammalian two-pore domain (K2P) K(+) channel important for mechanosens

174 Two-pore domain (K2P) K(+) channels are major regulators of

175 Two-pore domain (K2P) potassium channels are the major molec

176 Two-pore domain (K2P) potassium channels perform essential r

177 imal data suggest that stretch-activated two-pore-domain (K2P) K(+) channels play a critical role in

178 The pore domain keeps a well-defined conformation, whereas t

179 nt of the channel, whereas, in contrast, the pore domain lacks robust temperature sensitivity.

180 have observed conformational changes in the pore domain leading to asymmetrical collapses of the act

181 t found within the 5' UTR of the potassium 2-pore domain leak channel Task3 mRNA.

182 K(2P)2.1 (TREK-1) is a polymodal two-pore domain leak potassium channel that responds to exte

183 -gated Hv1 proton channels lack a homologous pore domain, leaving the location of the pore unknown.

184 ctural connections between the propeller and pore domains located close to lipid-binding sites.

185 hrough, while the channel pore formed by the pore domains mediates ion permeation.

186 ols the conformation of gates located in the pore domain (membrane segments S5-S6).

187 y altered macroscopic desensitization, and a pore domain mutation prolonged deactivation despite bloc

188 solic nucleotide binding domains (NBDs), but pore-domain mutations may also impair gating.

189 ctures have been solved for the transbilayer pore domain of a bacterial K+ channel and the tetrameris

190 d-binding domain of one subunit can gate the pore domain of an adjacent subunit.

191 e conserved aromatic residue near the cation pore domain of claudins contributes to cation selectivit

192 ural basis of Kvbeta1.3 interaction with the pore domain of Kv1.5 channels.

193 Ala-scanning mutagenesis of the pore domain of Kv1.5 identified the amino acids Thr479,

194 By searching sequence databases with the M2 pore domain of ligand-gated anion channels, we identifie

195 Here we report the structure of the pore domain of MCU from Caenorhabditis elegans, determin

196 e investigated specific lipid binding to the pore domain of potassium channels KcsA and chimeric KcsA

197 the structural architecture typified by the pore domain of potassium channels.

198 lasmic domain tightly controls gating of the pore domain of RyR1 to release Ca(2+).

199 ectifier) channels, as well as models of the pore domain of Shaker in the open and closed state.

200 ring structure that completely surrounds the pore domain of the channel.

201 into a homology model of the homo-tetrameric pore domain of the hERG potassium channel to identify st

202 he structural basis for their binding to the pore domain of the hERG1 channel.

203 The autoantibody against the pore domain of the L-type voltage-gated calcium channel

204 The pore domain of the nicotinic acetylcholine receptor has

205 tional knockout mouse strain by deleting the pore domain of TRPM8 and demonstrated that eTRPM8 knocko

206 r dynamics simulations of the open-activated pore domain of TRPV1 in the presence of three cationic s

207 Here we show that transplanting the pore domain of TRPV1 into Shaker gives rise to functiona

208 sA, a bacterial K+ channel homologous to the pore domain of voltage-gated K+ channels, provides a sta

209 The pore domain of voltage-gated potassium (Kv) channels con

210 -linker, located between voltage-sensing and pore domains of adjacent subunits.

211 fies the interface between the catalytic and pore domains of CFTR and that this modification facilita

212 the crevice between the voltage-sensing and pore domains of K(V) channels, making significant contac

213 ing representation of the voltage sensor and pore domains of the prokaryotic Na channel, NaChBac.

214 tion that the X-ray structure exhibits a low pore domain-opening propensity further supports this not

215 .1 channel alpha-subunit without the channel pore domain or the voltage sensor.

216 f the VSD, which drives gating in a separate pore domain, or, in channels lacking a pore domain, dire

217 ated cation channels composed of one central pore domain (PD) and four peripheral ligand-binding doma

218 otassium, and calcium channels are made of a pore domain (PD) controlled by four voltage-sensing doma

219 owever, uncoupling the Shaker K(+) channel's pore domain (PD) from the VSD prevented the mode-shift o

220 nsing domain (VSD) and the last two form the pore domain (PD).

221 e sensors (VSD) endow voltage-sensitivity to pore domains (PDs) through a not fully understood mechan

222 nsist of eight transmembrane domains and two pore domains per subunit organized in dimers.

223 ere, we present evidence implicating the two-pore domain, pH-sensitive TASK-1 channel as a target for

224 5 linker, which joins the voltage sensor and pore domains, plays a critical role in this slow deactiv

225 ain crystal structure can be docked onto the pore domain portion of the full-length KvAP crystal stru

226 Two-pore domain potassium (K(+)) channels (K2P channels) con

227 TREK-1 is a member of the two-pore domain potassium (K(2P)) channel family that is mec

228 potassium (TASK) channels-members of the two pore domain potassium (K(2P)) channel family-are found i

229 Two-pore domain potassium (K(2P)) channels are considered to

230 Two-pore domain potassium (K(2P)) channels play fundamental

231 Two-pore domain potassium (K2P) channel ion conductance is r

232 A cDNA encoding a two-pore domain potassium (K2p) channel subunit, AcK2p2, was

233 TREK-2 (KCNK10/K2P10), a two-pore domain potassium (K2P) channel, is gated by multipl

234 Two-pore domain potassium (K2P) channels act to maintain cel

235 tter understanding of the gating of TREK two pore domain potassium (K2P) channels and their activatio

236 TASK3 two-pore domain potassium (K2P) channels are responsible for

237 Polymodal thermo- and mechanosensitive two-pore domain potassium (K2P) channels of the TREK subfami

238 The two-pore domain potassium channel (K(2P)-channel) THIK-1 has

239 y P2Y1 receptor-mediated inhibition of a two-pore domain potassium channel and A1 receptor-mediated o

240 TASK channels belong to the two-pore domain potassium channel family and are modulated b

241 1) potassium channels are members of the two-pore domain potassium channel family and contribute to b

242 3) and TASK-3 (KCNK9) are members of the two-pore domain potassium channel family and form either hom

243 s the existence of a subfamily in the tandem pore domain potassium channel family with weak inward re

244 or "leak" current and is a member of the two-pore domain potassium channel family.

245 KCNK3, the gene that encodes the two pore domain potassium channel TASK-1 (K2P3.1), has been

246 ny similarities with current through the two-pore domain potassium channel TASK-1 and which is inhibi

247 epsilon-dependent phosphorylation of the two-pore domain potassium channel TASK-1.

248 ther selective increased activation of the 2-pore domain potassium channel TRESK (2-pore-domain weak

249 Of these families, the tandem pore domain potassium channels are a new and distinct cl

250 K(+) channel-1) (K(2P)3.1) atrial-specific 2-pore domain potassium channels is enhanced, resulting in

251 Two-pore-domain potassium (2-PK) channels have been shown to

252 Two-pore-domain potassium (K(+)) channels are substrates for

253 Two-pore-domain potassium (K(2P)) channels are key regulator

254 Two pore-domain potassium (K(2P)) channels mediate potassium

255 Two-pore-domain potassium (K2P) channels are responsible for

256 the thermosensitive and mechanosensitive two-pore-domain potassium (K2P) channels, are clustered at N

257 nervous system are often carried through two-pore-domain potassium (K2P) channels.

258 tein that interacts with a member of the two-pore-domain potassium channel family and is involved in

259 3) potassium channels are members of the two-pore-domain potassium channel family.

260 tage-independent leak currents through a two-pore-domain potassium channel that we term Sandman.

261 Here, we identify a two-pore-domain potassium channel, KCNK3, as a built-in rheo

262 Two-pore-domain potassium channels (K(2P)) are the major det

263 Two-pore-domain potassium channels are a family of ion chann

264 osensitive ion channels (channels of the two-pore-domain potassium family (K2P) including TREK-1, TRE

265 d' transmits force via a linker to the S5-S6 pore domain 'receptor', thereby opening or closing the c

266 e S4-S5 linker that reposition the S1-S4 and pore domains relative to the TRP helix, leading us to pr

267 e focused on the agonist binding and channel pore domains, relatively little is known about the role

268 brane voltages, to opening or closing of the pore domain's ion channel remains unresolved.

269 potassium channels, but the ion selectivity pore domain sequence resembles that of a Ca(v) channel.

270 of the voltage-sensing domains couple to the pore domain so as to gate ion conduction is not understo

271 channel encoded by the potassium channel, 2-pore domain, subfamily K, member 3 (Kcnk3) gene] correla

272 ture cluster away from the interface between pore domain subunits.

273 regions near the interface between adjacent pore domain subunits.

274 interface between the voltage sensor and the pore domain such that the channels now open upon depolar

275 semble as tetramers with a centrally located pore domain surrounded by a voltage-sensing domain (VSD)

276 ain in prokaryotic channels is closer to the pore domain than in the K(V)1.2 structure.

277 detergent and liposomes, for residues at the pore domain that agree with their location in the TRPV1

278 ined by the identity of a residue within the pore domain that can be altered through RNA editing.

279 potassium (K(v)) channels contain a central pore domain that is partially surrounded by four voltage

280 etween the pore helix and outer helix of the pore domain that occurs early in the transition from ope

281 ttributable to conformational changes in the pore domain that stabilize the open state of the channel

282 domains, but sequence alignment indicated a pore domain that was unlike the consensus domains in K+

283 voltage sensing domain in the absence of the pore domain, the Shaker Kv channel was truncated after t

284 els and in other membrane proteins that lack pore domains, the extent to which their voltage-sensing

285 th their voltage sensor domains connected to pore domains, the HCS in the voltage sensor domain allow

286 librium constant for the voltage-independent pore domain to favor a closed pore, as well as reducing

287 dy, we mutated residues throughout the TRPV1 pore domain to identify loci that contribute to dynamic

288 5 linker connects nearby voltage-sensing and pore domains to produce a non-domain-swapped transmembra

289 III and DIV are important for coupling their pore domains to their voltage-sensor domains, and that A

290 s-Ned-19 acts allosterically by clamping the pore domains to VSD2.

291 voltage-sensing domain (VSD) and lacking the pore domain typical of other voltage-gated ion channels.

292 s of surface-exposed S5 residues of the KAT1 pore domain, we have screened randomly mutagenized libra

293 n close physical proximity to the C-terminal pore domain, we prepared microsomal membranes from COS-7

294 the 2-pore domain potassium channel TRESK (2-pore-domain weak inward-rectifying potassium channel-rel

295 t mutations surrounding the putative channel pore domain were expressed and characterized in Xenopus

296 All these other channels also contain a pore domain, which forms a central pore at the interface

297 detect changes in transmembrane voltage, and pore domains, which conduct ions.

298 two protomers, each containing two distinct pore domains, which create a two-fold symmetric K(+) cha

299 lecule reclines in the central cavity of the pore domain, with the wide end inserting into the fenest

300 bolished by a point mutation in the putative pore domain without altering current magnitude.

301 Although KcsA contains only a pore domain, without voltage-sensing machinery, it has t