Thr339-to-serine substitution in rat P2X2 receptor second transmembrane domain causes constitutive opening and indicates a gating role for Lys308.
about
Polar residues in the second transmembrane domain of the rat P2X2 receptor that affect spontaneous gating, unitary conductance, and rectificationInsights into the channel gating of P2X receptors from structures, dynamics and small moleculesExploring the ATP-binding site of P2X receptorsInsights into the Molecular Mechanisms Underlying Mammalian P2X7 Receptor Functions and Contributions in Diseases, Revealed by Structural Modeling and Single Nucleotide PolymorphismsRole of the domain encompassing Arg304-Ile328 in rat P2X2 receptor conformation revealed by alterations in complex glycosylation at Asn298Tightening of the ATP-binding sites induces the opening of P2X receptor channelsP2X receptors: dawn of the post-structure era.Signal transmission within the P2X2 trimeric receptor.Gated access to the pore of a P2X receptor: structural implications for closed-open transitions.Pore-opening mechanism in trimeric P2X receptor channelsCovalent modification of mutant rat P2X2 receptors with a thiol-reactive fluorophore allows channel activation by zinc or acidic pH without ATP.Allosteric modulation of Ca2+ flux in ligand-gated cation channel (P2X4) by actions on lateral portalsInvolvement of the cysteine-rich head domain in activation and desensitization of the P2X1 receptor.Photo-switchable tweezers illuminate pore-opening motions of an ATP-gated P2X ion channelCysteine substitution mutagenesis and the effects of methanethiosulfonate reagents at P2X2 and P2X4 receptors support a core common mode of ATP action at P2X receptors.Gating the pore of P2X receptor channelsOptical control of an ion channel gateNew structure enlivens interest in P2X receptors.Structural interpretation of P2X receptor mutagenesis studies on drug actionP2X receptors as drug targets.Key sites for P2X receptor function and multimerization: overview of mutagenesis studies on a structural basis.The P2X1 receptor and platelet function.P2X Receptor Activation.Functional relevance of aromatic residues in the first transmembrane domain of P2X receptors.Molecular basis of selective antagonism of the P2X1 receptor for ATP by NF449 and suramin: contribution of basic amino acids in the cysteine-rich loop.Mechanistic insights from resolving ligand-dependent kinetics of conformational changes at ATP-gated P2X1R ion channels.Contribution of the region Glu181 to Val200 of the extracellular loop of the human P2X1 receptor to agonist binding and gating revealed using cysteine scanning mutagenesis.P2X receptor channels show threefold symmetry in ionic charge selectivity and unitary conductance.Direct gating of ATP-activated ion channels (P2X2 receptors) by lipophilic attachment at the outer end of the second transmembrane domainP2X receptor chimeras highlight roles of the amino terminus to partial agonist efficacy, the carboxyl terminus to recovery from desensitization, and independent regulation of channel transitionsP2X receptor intermediate activation states have altered nucleotide selectivity.Functional and structural identification of amino acid residues of the P2X2 receptor channel critical for the voltage- and [ATP]-dependent gating.
P2860
Q24648191-B6EA8EAE-AAA8-4257-94BD-67999B8C1455Q26771359-A9558886-29F5-416D-849C-9F4376343AC7Q26852221-AEC3BC2E-AAC6-41A3-97FF-5695988C74E7Q27500422-B58315BC-B439-48AD-8856-74ED9F6AF214Q28570546-0CE5B408-F033-4F8A-8ED1-835F13DA3FC3Q30513952-A33F8DEA-0014-4379-AA4A-D07F4342C8AEQ33511146-796B685A-2CDA-43EA-8DC2-A8B85B69DB23Q33672907-D9951B57-BC00-406F-9863-9C83CAE33B9CQ33744436-A38D2A95-B9AD-450E-A06D-644DBA28E367Q34313783-A0B2F418-4958-4763-80C9-917915C5A274Q34462141-E04EC936-1D2B-49AA-9097-B96DE6085857Q35801949-253D2EBE-82DA-424A-90C9-C9AB672B1CE7Q36094216-D002800A-E8E8-4478-9764-96B94AB4A049Q36539721-958FD198-56FF-4C5F-9A50-C44006CB41CDQ36761837-92BED9EB-A3F5-4FCF-83B3-E733E02AD299Q37069023-0790452C-4D91-4078-B17D-D5A57CF0785AQ37409444-CD69B85F-D5CA-4279-A83C-D92EA2133EDDQ37708660-6A8B799B-6B19-4FA7-95CE-08B571BD69C8Q37803250-D9827346-CD7F-47B2-911F-6C0F1CF471B7Q38068620-E2B7F95D-73BD-470E-BE5D-BDE92E5D6131Q38273638-ADF17E13-EE3A-40CB-BDF1-3F8E2D3184BBQ38306728-546C7FB4-CB4A-4894-A592-3FB3379E801DQ39390185-1C2E54B4-1DCC-4772-891D-4125D0B53C52Q39854925-8266D5F1-40DE-4DFE-B1A3-A5809547A7DEQ40725974-8970A35A-BD3F-4932-B1D5-044407DD96A0Q41063256-50B57C3D-A2C1-4977-918F-A4E6E706485EQ41502656-287B9CE1-CF6A-487A-A588-E02DE2387BD9Q41526271-902BCF22-20C9-460A-97CE-76567AB71496Q41863359-770C4C6A-9CA7-4201-AD09-5561D2B1AE79Q42005371-701B80B6-2D81-4A17-9EC4-E6F0D5E12503Q42604461-1310AE60-C371-4F0B-A5A3-E860923847AAQ43250084-C411F131-9242-4038-B543-B9ECB6ADAD76
P2860
Thr339-to-serine substitution in rat P2X2 receptor second transmembrane domain causes constitutive opening and indicates a gating role for Lys308.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Thr339-to-serine substitution ...... ates a gating role for Lys308.
@en
type
label
Thr339-to-serine substitution ...... ates a gating role for Lys308.
@en
prefLabel
Thr339-to-serine substitution ...... ates a gating role for Lys308.
@en
P2093
P1476
Thr339-to-serine substitution ...... ates a gating role for Lys308.
@en
P2093
Helen E Broomhead
Lishuang Cao
R Alan North
Samuel J Fountain
P304
12916-12923
P356
10.1523/JNEUROSCI.4036-07.2007
P407
P577
2007-11-01T00:00:00Z