ライフサイエンスコーパス: pore domain

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

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

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

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

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

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

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

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

9 This study concerns the pore domain.

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

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

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

13 ing between the extracellular domain and the pore domain.

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

15 modeled after the crystal structure of KvAP pore domain.

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

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

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

19 connect the nucleotide binding pocket to the pore domain.

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

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

22 nts to control ionic conductance through the pore domain.

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

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

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

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

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

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

29 vents strong nonannular lipid binding to the pore domain.

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

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

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

33 uctural link between the voltage sensing and pore domains.

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

35 uggested an interaction between neighbouring pore domains.

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

37 at functionally links the ligand binding and pore domains.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

100 The pore domain is missing in Hv1.

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

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

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

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

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

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

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

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

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

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

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

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

113 (<5% O2), in addition to inhibiting the two-pore domain K(+) channels TASK-1/3 (TASK), indirectly ac

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

168 The pore domain of the nicotinic acetylcholine receptor has

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

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

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

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

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

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

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

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

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

178 .1 channel alpha-subunit without the channel pore domain or the voltage sensor.

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

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

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

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

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

184 5 linker, which joins the voltage sensor and pore domains, plays a critical role in this slow deactiv

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

221 regions near the interface between adjacent pore domain subunits.

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

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

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

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

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

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

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

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

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

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

232 5 linker connects nearby voltage-sensing and pore domains to produce a non-domain-swapped transmembra

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

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

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

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

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

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

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

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

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

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

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

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