ライフサイエンスコーパス: protomer

1 2' bind to sites 2 and 2' on FnIII-1 of each protomer.

2 ccess and deep drug binding pockets in every protomer.

3 aining at least 26 transmembrane helices per protomer.

4 operativity in hydrolysis of the ATP in each protomer.

5 47 in transmembrane helix 5) in the adjacent protomer.

6 d action of residues from more than a single protomer.

7 regulator SczA, and binds two zinc ions per protomer.

8 rimers with transmembrane pores through each protomer.

9 one protomer is sensed by a second symmetric protomer.

10 of the C-terminal helix alpha9 of the second protomer.

11 e lig1 state and isotopic labeling of either protomer.

12 ntaining F surface residues on a neighboring protomer.

13 ne 5'-O-(3-thiotriphosphate) (ATPgammaS) per protomer.

14 e with a single transmembrane domain in each protomer.

15 s bound to both the D1 and D2 domains of the protomer.

16 ing that incorporation requires a Spr28-Spr3 protomer.

17 odulate the binding of dopamine at the other protomer.

18 ion and approximately 5,000 residues in each protomer.

19 in asymmetric dimers containing only one Pfr protomer.

20 inhibit the binding of dopamine at the other protomer.

21 three different conformations of the active protomer.

22 acellular ends of TM2 and TM7 within the D2R protomer.

23 ensor I motif (285)REDXXYR(291) of the trans protomer.

24 o the cytosol through the cavity within each protomer.

25 us is not blocked by an adjacent tropomyosin protomer.

26 urbation is in the order of 6-7 kcal/mol per protomer.

27 primary proton acceptor D97 within the same protomer.

28 bs, enabling them to reach an adjacent gp120 protomer.

29 shion, with a Sub2 molecule attached to each protomer.

30 nds across two adjacent envelope (E) protein protomers.

31 1:2:1 stoichiometry-which form two identical protomers.

32 HA trimer stem at the interface between two protomers.

33 recognize a conserved cavity formed by two F protomers.

34 otomers and the new finding of cephalosporin protomers.

35 ve and negative cooperativity among its four protomers.

36 studies identify allosteric pathways between protomers.

37 eractions within and between the constituent protomers.

38 n its surface and the C terminus of adjacent protomers.

39 ximal stimulation required occupancy of both protomers.

40 n a protomer and mediates key contacts among protomers.

41 omeric state composed of two subunits of six protomers.

42 tion through contacts made with two adjacent protomers.

43 moieties interact with different KstR2(Mtb) protomers.

44 o the HA stem to covalently bridge the three protomers.

45 the HSS contributes to communication between protomers.

46 C-terminal (CTD) domains of its successive N protomers.

47 bind to the alpha subunit of pump alphabeta protomers.

48 between the zinc-binding domain and adjacent protomers.

49 n and the J-domain in one of the RIIbeta:J-C protomers.

50 consecutive residues coordinated by adjacent protomers.

51 g cavity through lateral gates between TatBC protomers.

52 targets an antigenic site incorporating two protomers.

53 stoichiometry in solution is 4 TreS + 2 Pep2 protomers.

54 lectrostatic charges between the neighboring protomers.

55 tecture and stabilizing membrane-bound Sec18 protomers.

56 actions, and two conformations of gp120-gp41 protomers (A and B protomers in AAB and ABB trimers) tha

57 ural details of a filament composed of Vps32 protomers, a major component of ESCRT-III complexes.

58 sharing critical residues from two defective protomers across the heteromer interface.

59 f NTD up/down equilibria between neighboring protomers, allowing us to define interprotomer pathways

60 amers composed of 2alpha- and 2beta-tryptase protomers (alpha/beta-tryptase) form naturally in indivi

61 nd to sites 1 and 1', formed by L1 of one IR protomer and alpha-CT and FnIII-1 of the other.

62 with the first triple-helix bundle within a protomer and mediates key contacts among protomers.

63 mutated PTHR bind retromer through the VPS26 protomer and sequentially assemble a ternary complex wit

64 formed by the L1 and CR domains of one IGF1R protomer and the alpha-CT and FnIII-1 domains of the oth

65 the N-terminal conformational change of one protomer and the displacement of the C-terminal helix al

66 pying equivalent hydrophobic pockets in each protomer and their CoA moieties adopting non-equivalent

67 nus of DGAT1 interacts with the neighbouring protomer and these interactions are required for enzymat

68 zation differs between the strand-separating protomer and those bound to the single-stranded region.

69 We biochemically reconstituted NPC core protomers and elucidated the underlying protein-protein

70 imerisation via sub-domain exchanges between protomers and highlights nucleotide positions in a conti

71 McrC interacts asymmetrically with McrB protomers and inserts a stalk into the pore of the ring,

72 at the filament contains between 7 and 9 Arp protomers and is capped at both ends.

73 0 homologs, is due to buckling of one of the protomers and is most pronounced at the broadly conserve

74 t the maturation complex is composed of four protomers and one IHF heterodimer bound at the cos site.

75 into final protein products, and assembly of protomers and pentamers in infected M1-D macrophages did

76 identified ab8 interactions with all three S protomers and showed how ab8 neutralized the virus by di

77 also induces conformational changes in Sec18 protomers and that hexameric Sec18 cannot bind PA membra

78 otomers, including the known fluoroquinolone protomers and the new finding of cephalosporin protomers

79 terface, but the relative orientation of the protomers and their contacts differ substantially.

80 tA motif, connecting the active sites of two protomers and thereby modulating the cooperative interac

81 r is nearly identical to that of the F-actin protomer, and in vitro polymerization assays show that t

82 to the heavy and light chains of mature MPO protomers, and (iii) three covalent bonds between heme a

83 helix folds and AAA+ modules of neighbouring protomers, and a quasi-spiral arrangement of DNA binding

84 als that the antibody binds between two gp41 protomers, and neutralizes the virus by accelerating tri

85 binding interfaces, on the LukG and the LukH protomers, and show that human CD11b-I induces LukGH oli

86 contact peptide residues from all three Env protomers, and thus explains its highly trimer-specific

87 H2B acidic patch, distal to the active SNF2h protomer, appear disordered.

88 We show that a monomeric protein (protomer) appropriately modified with biologically inspi

89 e CARD and the WD40 repeats of a nearby Dark protomer are indispensable for Dronc activation.

90 , focused on homohexameric constructs, where protomers are either entirely WT or contain a disease-ca

91 sults suggest that physical contacts between protomers are important for the substrate-induced change

92 The structure shows that four Ptch1 protomers are organized as a loose dimer of dimers.

93 brane-proximal domains from the two PlexinC1 protomers are placed close to each other, poised to prom

94 Additional Crc protomers are recruited to the core to generate higher-o

95 The gp120 protomers are rotated and separated in the CD4-bound str

96 To validate our structure, we probed the protomer arrangement by solvent paramagnetic resonance e

97 rms a helix-helix interaction that links the protomers as a unique feature of AfFabI.

98 le conformer simulations of crystallographic protomers as described in the companion article.

99 nits is partially restored by neighboring WT protomers, as is the two-pronged binding of the UBXD1 ad

100 The residue H75 defines a cross-protomer Asp-His-Trp triad, which potentially serves as

101 in human cells have established that septin protomers assemble into linear hetero-octameric rods wit

102 This protomer assembles into a functional higher-order comple

103 d functionality of the chloride ion-mediated protomer assembly by using a single-chain technology to

104 model that describes the effects of salt on protomer assembly into a tetrameric complex.

105 le possible helix interfaces mediating inter-protomer associations.

106 ate was crosslinked in vivo to a second SecA protomer at its 1M6N interface, suggesting that this spe

107 trate/inhibitor-binding site of the opposite protomer at its carboxyl terminus.

108 Protomers at the spiral seam undergo nucleotide-specific

109 that assessed interactions between receptor protomers at the surface of transfected cells indicated

110 most efficiently as a dimer, yet how the two protomers avoid a tug-of-war is unclear.

111 pposite sides of a nucleosome, but how these protomers avoid competition is unknown.

112 Molecular simulations indicate that when the protomers become inward-facing, they cause deep, long-ra

113 ng a central dimer, and the two ChsH2(DUF35) protomers being at the periphery.

114 Two protomers bind the single-stranded region of RNA substra

115 ke ID structure through the ubiquitin of one protomer binding to the other protomer in a reciprocal f

116 The isolated protomer binds DNA weakly and does not discriminate betw

117 XRCC4 phosphorylation and that only one PNKP protomer binds per XRCC4 dimer.

118 ve long-range attractive force on individual protomers, both long-range lipid order and interface for

119 ict bends the helices until the helix of one protomer breaks to relieve the repulsion.

120 The N-terminal subunit of each S protomer, called S1, folds into four distinct domains de

121 Specifically, results suggest that D3 protomers can interact with each other via at least two

122 The ESX-3 protomer complex is assembled from a single copy of the

123 Each protomer comprises six transmembrane segments (TMs), wit

124 er-length distribution adjusts to changes in protomer concentration and affinity.

125 em stands out in that the dependency of Q on protomer concentration switches from being dominated by

126 d in that Q decreases with half the power in protomer concentration than for any multivalent scaffold

127 empirical aggregation data composed of total protomer concentrations and fibril length distributions

128 During catalysis, the protomer conformational exchange rate becomes enhanced,

129 We find that the 5 TcA protomers conformationally adapt to fit around the cocoo

130 Each protomer consists of nine transmembrane segments, which

131 that symmetric activation with two Pfr state protomers constitutes the signaling-active species.

132 Displacement of cis-protomer contacts from the apo state is rate-limiting fo

133 a heavy-chain insertion and increased inter-protomer contacts.

134 crystallized as a symmetric dimer, with each protomer containing a putative proton channel.

135 MacB forms a dimer in which each protomer contains a nucleotide-binding domain and four t

136 echocystis, showing a tetramer in which each protomer contributes two helices to a membrane-spanning

137 We show that IHF and the terminase protomer cooperatively assemble at the cos site and that

138 key residues in substrate translocation and protomer crosstalk.

139 model to all 3,757 ordered residues in each protomer, defining the transmembrane pore in unprecedent

140 h distinct N-glycan conformations across Env protomers, demonstrating intra-Env glycan heterogeneity.

141 Protomers disassembled from both the barbed and pointed

142 Inter-protomer distance correlates with rotation of an alpha-h

143 studies, oligomers are assembled using inter-protomer distance restraints.

144 6-MDa molecular mass assembly containing six protomers each of two different subunits, Fas1 (beta) an

145 These were found to consist of adjacent protomers engaging the interdomain linker of one molecul

146 These mAbs recognize an inter-protomer epitope in the GP fusion loop, a critical and c

147 dimers, ligands bind and activate the 5-HT2C protomer exclusively.

148 al exchange rate becomes enhanced, the empty protomer exhibits increased local disorder, and water eg

149 The two receptor protomers, extracellular domain and amino terminal fragm

150 In the dimer, the protomers faced each other through the F and G alpha-hel

151 ilament architectures are not limited by the protomer fold.

152 dimer interface and cap domain, priming one protomer for substrate binding.

153 Thirteen protomers form a large periplasmic domain of six stacked

154 In the structure, the protomers form a stable dimer that is consistent with as

155 entameric, with the N-terminal region of the protomer forming an extensive set of contacts across sev

156 etabetaalpha organization, with the two Ltp2 protomers forming a central dimer, and the two ChsH2(DUF

157 in longitudinally between two adjacent actin protomers forming what is called a decorative interactio

158 at completes the active site from a distinct protomer, forming contacts with the gamma-phosphate of t

159 ce, simultaneously interacting with three CA protomers from adjacent hexamers via two noncanonical in

160 a well-established phenomenon that can alter protomer function.

161 e a model for transport mechanism where CmeB protomers function independently within the trimer.Multi

162 in pleiotropic signaling, yet how individual protomers function within oligomers remains poorly under

163 These dimers ("protomers") further assemble into a low-rise left-handed

164 tion step occurred sequentially in the three protomers, generating two asymmetric oligomer intermedia

165 We find that Panx1 protomers harbor four transmembrane helices similar in a

166 Each DGAT1 protomer has nine transmembrane helices, eight of which

167 For this purpose, differently labeled protomers have been assembled into the full pentamer com

168 iquitin of one protomer binding to the other protomer in a reciprocal fashion.

169 Each protomer in GltPh consists of a trimerization domain inv

170 TPases, buries the carboxyl terminus of each protomer in the central channel of the hexamer and hinde

171 coelicolor GlgEs, reported before, with each protomer in the homodimer comprising five domains.

172 trometry indicated that a loss of 4-5 kJ/mol/protomer in the N3 domain that is peripheral to the memb

173 thesis of functional coupling of two SERCA2a protomers in a dimer that reduces the energy barrier of

174 nformations of gp120-gp41 protomers (A and B protomers in AAB and ABB trimers) that differ in their d

175 specific spatial organizations of individual protomers in complexes where the ratiometric composition

176 ional differences in active and inactive Cre protomers in crystallographic tetramers.

177 ue for dissecting interactions of individual protomers in homo-oligomeric complexes.

178 inhibits all RAF isoforms and occupies both protomers in RAF dimers.

179 rences are observed at the interface between protomers in the crystal structure of the PCNA-K20ac rin

180 in-swapped, cross-armed conformation for the protomers in the dimeric protein.

181 e curves indicated that the occupancy of the protomers in the Env trimer governs viral activation ver

182 a strict division of labor between the Ded1p protomers in the oligomer.

183 r several antibiotic species due to multiple protomers, including the known fluoroquinolone protomers

184 with the trimerization of alpha-chains into protomers inside the cell, which then are secreted and u

185 ex formed in the membrane via specific cross-protomer interactions plays a role in its functional mec

186 arge rearrangements at the cytoplasmic inter-protomer interface and that this motion triggers couplin

187 The cytoplasmic inter-protomer interface is unique and consists of a CTD coile

188 ghly conserved residue H75 is located at the protomer interface.

189 could identify specific interactions at the protomer interfaces, if the sensitivity is enhanced by d

190 I on the hMPV F protein and incorporates two protomers into its epitope yet is unique from previously

191 tch by the IGL loop of the lowest positioned protomer, involving release and re-engagement with the c

192 The lambda-terminase protomer is composed of one large catalytic subunit tigh

193 The binding of six nucleotides per protomer is consistent with the "rule of six" that gover

194 One protomer is in the outside-facing state.

195 bition of the second protomer when the first protomer is occupied, comprising a novel class of dimer

196 l allostery, in which a binding event in one protomer is sensed by a second symmetric protomer.

197 at this interface and the arrangement of two protomers is a prerequisite for the formation of the obs

198 The association of protomers is chloride-dependent, whereby chloride ions i

199 expression we find that BRET between beta2AR protomers is directly proportional to the density of the

200 loops at the trimeric interface of adjacent protomers is evident in the N197Q mutant by hydrogen-deu

201 ropose a transport mechanism where each CmeB protomers is functionally independent from the trimer.

202 The "breathing" of the HA protomers is implied by the exposure of this epitope, wh

203 The communication between the two protomers is mediated by an alpha-helix that interacts w

204 ealed that an intact catalytic cycle in both protomers is required for enhancing the efficacy of Ca(2

205 ve or independent, ATP hydrolysis on the two protomers is sequential and deterministic.

206 In the absence of DNA, six DnaC protomers latch onto and crack open a DnaB hexamer using

207 dimer inhibits phosphorylation in the second protomer, leading to ~50% phosphorylation of the availab

208 onserved histidine residue in the individual protomers, leading to diphosphorylation.

209 ptase protomers on neighboring beta-tryptase protomers likely result in the novel substrate repertoir

210 tched endogenous tobacco Rca levels (~1 umol protomer.m(2)) and enhanced RsRubisco activation to 75%

211 In this approach, the predetermined protomer model is subject to full angular and spatial se

212 BBL undergoes structural changes within each protomer; moreover, the individual m4-1BBL protomers rot

213 , is highly cooperative indicating that both protomers move in concert.

214 but the behavior can be exaggerated at small protomer numbers because of a maximal polymer size, anal

215 /ERK signaling" where transactivation of one protomer occurs as a result of drug inhibition of the ot

216 y demonstrated that SB269652 (1) engages one protomer of a dopamine D2 receptor (D2R) dimer in a bito

217 (SB269652) (1) adopts a bitopic pose at one protomer of a dopamine D2 receptor (D2R) dimer to negati

218 phosphorylation-site mutations into just one protomer of a Y1/Y1 BiFC homodimer had no impact on effi

219 dine tail to include a free cysteine on each protomer of model BG505 NFL trimers to allow covalent li

220 unidirectional transactivation of the 5-HT2C protomer of MT2/5-HT2C heteromers.

221 sides of SecB results in release of only one protomer of SecA yielding a complex of stoichiometry Sec

222 ooperativity, whereby phosphorylation in one protomer of the dimer inhibits phosphorylation in the se

223 trimer binding a coupling protein CheW and a protomer of the kinase dimer.

224 ssible counterpart D433 (located on the T1R2 protomer of the receptor) is safely large to avoid elect

225 hway may lie at or near the interface of the protomers of a BR trimer.

226 nt, functionally relevant cross talk between protomers of a microbial rhodopsin homo-oligomer.

227 ngly suggest that MCC22 acts by bridging the protomers of a MOR-CCR5 heteromer having a TM5,6 interfa

228 prises amino-acid residues from two adjacent protomers of HA.

229 hese RNPs, consisting of approximately 2,600 protomers of nucleocapsid (N) protein, form the template

230 a dimer of dimers, forms a complex with two protomers of SecA, which is the ATPase that provides ene

231 ex that binds Tat substrates, while multiple protomers of TatA assemble at substrate-bound TatBC rece

232 nside a channel-like passage between the two protomers of the dimer.

233 ith the companion subdomain in each brace of protomers of the DnaB hexamer.

234 nd in a wash-resistant manner to one or both protomers of the homodimer.

235 ,164 aa) forms a homodimer and binds to both protomers of the Hsp90 middle domain.

236 in also located within the interface between protomers of trimeric Lg-ECD, thereby explaining the def

237 PLY protomers oligomerize as rings on the membrane and then

238 Allosteric effects of alpha-tryptase protomers on neighboring beta-tryptase protomers likely

239 P is also responsible for bringing new N protomers onto the nascent RNA during genome replication

240 ransitions, with allosteric elements in each protomer orchestrating host receptor-induced exposure of

241 igomers with high-order stoichiometry (n > 2 protomers per homo-oligomer), but it was the monomeric f

242 lical filament of 103A pitch, comprising 6.4 protomers per turn, with a rise of 16.1A and a twist of

243 omplexes as asymmetric dimers, in which each protomer plays a specific role.

244 assessment of endocytosis of one coexpressed protomer population.

245 aces of the middle domains of opposing Hsp90 protomers prior to ATP-directed N-domain dimerization.

246 esembles a "nutcracker" with two L-terminase protomers projecting from the C-termini of an S-terminas

247 trol through the nucleosome, where one SNF2h protomer promotes asymmetric octamer deformation to inhi

248 d by the dimerization arm of the neighboring protomer, providing a structural basis for dimerization

249 alpha7, restricts the proximity of the trans-protomer required for Nt binding.

250 Whereas agonist binding to one protomer resulted in G protein activation, maximal stimu

251 hydrogen bonds with E553 on the neighboring protomer, resulting in the strengthening of the kindlin2

252 h protomer; moreover, the individual m4-1BBL protomers rotate relative to each other, yielding a dime

253 d mass of a protein complex consisting of 16 protomers, RuBisCO (517 kDa), is not affected by the num

254 sidues of the other protomer to disrupt that protomer's TPR-U-box tight binding interface, swiftly ex

255 The protomer shows a mirrored arrangement of the transmembra

256 one DnaK monomer contacts two adjacent ClpB protomers simultaneously.

257 ting how the RAD51-DNA interaction modulates protomer spacing and filament pitch.

258 ting that despite variations in sequence and protomer structure these proteins may share a common pat

259 PIV5-N protomer subdomains are very similar in structure to the

260 ts up differential hydrolysis rates for each protomer, such that the buckled conformation favors ATP

261 mer assembly, model how interactions between protomers support heptamer formation, and identify surfa

262 ring eight structurally distinct types of IN protomers supporting two catalytically competent subunit

263 Under force, R577 on one protomer switches from interacting with S550 to forming

264 igomerization and identifies regions of VacA protomers that are predicted to contact the host cell su

265 l channel comprised of a hexameric spiral of protomers that contact substrate via conserved pore-loop

266 Formation of native PulD-multimers by mixing protomers that differ in N3 domain stability, suggested

267 Cross-sensitization of Env protomers that do not bind the CD4mc to neutralization b

268 comprised of three TNF homology domain (THD) protomers that mimic tmTNF.

269 om [2 Fe:9 Zn:6 protomers] to [8 Fe:21 Zn:12 protomers], these protein cages represent some of the co

270 distribution of electrons between functional protomers through a subunit-bridging FeS cluster.

271 rters form homodimers, with each beta-barrel protomer tightly capped by SusD.

272 demonstrating that release requires only one protomer to be functional in stimulating BiP ATPase acti

273 forces the C-terminal residues of the other protomer to disrupt that protomer's TPR-U-box tight bind

274 ed region of RNA substrates and load a third protomer to the duplex, which then separates the strands

275 Instead, the antibody binds between HA head protomers to an epitope that must be partly or transient

276 FMNAT catalytic sites of the two neighboring protomers to approach, in agreement with active site res

277 The model shows one of the protomers to be rotated and tilted outward at the tip en

278 ty, resulting in coassembly of mutant and WT protomers to form an enzyme with reduced activity.

279 th stoichiometries ranging from [2 Fe:9 Zn:6 protomers] to [8 Fe:21 Zn:12 protomers], these protein c

280 eby chloride ions induce interactions of the protomers' trimeric NC1 domains leading to NC1 hexamer f

281 RsbR and RsbS are organized in a 60-protomers truncated icosahedron.

282 eries of constructs in which only one of the protomer types is NMR-labeled.

283 Two protomers undergo a ratchet-like conformational change t

284 This dominant effect on the associated protomer was also observed in neurons, supporting the ph

285 A physical interaction between the protomers was confirmed using high resolution cryogenic

286 Virus was inactivated when all three Env protomers were occupied by the CD4mc, and gp120 shedding

287 mers, with enhanced inhibition of the second protomer when the first protomer is occupied, comprising

288 gene encodes 22 N-linked glycan sequons per protomer, which likely play a role in protein folding an

289 g leads to conformational changes within the protomer, which might propagate within the ring structur

290 n from the monomer to the assembly-competent protomer, which then oligomerizes rapidly to active pore

291 elated rigid body rocking motion of the four protomers, which drives the T to R transition.

292 The structural versatility of the four P protomers-which are largely disordered in their free sta

293 atch is expected to inhibit the second SNF2h protomer, while disorder near the dyad is expected to pr

294 ic octamer deformation to inhibit the second protomer, while stimulating directional DNA translocatio

295 It is a dimer of seven-subunit protomers with 50 trans-membrane helices each.

296 eotides precisely are associated with each N protomer, with alternating three-base-in three-base-out

297 nteractions using induced multimerization of protomers within such complexes, at constant expression.

298 cific side chain contributions from adjacent protomers within the complex.

299 at the macromolecular interface between two protomers within the trimer.

300 We show unambiguously that individual protomers within the trimeric transporter function fully