Identification of two amino acids of the human cholecystokinin-A receptor that interact with the N-terminal moiety of cholecystokinin.
about
Arginine 197 of the cholecystokinin-A receptor binding site interacts with the sulfate of the peptide agonist cholecystokininEvidence for a direct interaction between the penultimate aspartic acid of cholecystokinin and histidine 207, located in the second extracellular loop of the cholecystokinin B receptorDistinct molecular mechanisms for agonist peptide binding to types A and B cholecystokinin receptors demonstrated using fluorescence spectroscopyCholecystokinin receptors in Atlantic salmon: molecular cloning, gene expression, and structural basis.Cross-interactions of two p38 mitogen-activated protein (MAP) kinase inhibitors and two cholecystokinin (CCK) receptor antagonists with the CCK1 receptor and p38 MAP kinase.Structure of cholecystokinin receptor binding sites and mechanism of activation/inactivation by agonists/antagonists.Arginine 336 and asparagine 333 of the human cholecystokinin-A receptor binding site interact with the penultimate aspartic acid and the C-terminal amide of cholecystokinin.Probing a model of a GPCR/ligand complex in an explicit membrane environment: the human cholecystokinin-1 receptor.Peptide hormone binding to G-protein-coupled receptors: structural characterization via NMR techniques.Met-195 of the cholecystokinin-A receptor interacts with the sulfated tyrosine of cholecystokinin and is crucial for receptor transition to high affinity state.Molecular basis of agonist binding to the type A cholecystokinin receptor.Moleular models for cholecystokinin-A receptor.Use of multidimensional fluorescence resonance energy transfer to establish the orientation of cholecystokinin docked at the type A cholecystokinin receptor.Structural basis of cholecystokinin receptor binding and regulation.Cholecystokinin 1 receptor modulates the MEKK1-induced c-Jun trans-activation: structural requirements of the receptor.Direct identification of a distinct site of interaction between the carboxyl-terminal residue of cholecystokinin and the type A cholecystokinin receptor using photoaffinity labeling.Flexibility and extracellular opening determine the interaction between ligands and insect sulfakinin receptors.Synthesis and solution characterization of a porphyrin-CCK8 conjugate.The biologically crucial C terminus of cholecystokinin and the non-peptide agonist SR-146,131 share a common binding site in the human CCK1 receptor. Evidence for a crucial role of Met-121 in the activation process.Environment and mobility of a series of fluorescent reporters at the amino terminus of structurally related peptide agonists and antagonists bound to the cholecystokinin receptor.CCK8 peptide derivatized with diphenylphosphine for rhenium labelling: synthesis and molecular mechanics calculations.The Human Orexin/Hypocretin Receptor Crystal Structures.Fluorescent indicators distributed throughout the pharmacophore of cholecystokinin provide insights into distinct modes of binding and activation of type A and B cholecystokinin receptors.
P2860
Q24672870-A43897B0-A4F4-477E-BA1D-0EBDB4067E3FQ28141454-FB67CDAB-CA6E-432E-A866-1928F782D1C0Q28291059-05E99B12-1B28-4BE7-B443-81D0C1B6367FQ30356359-1F8A036B-70A8-456D-B3CB-149D0AE95D3DQ30984991-1177A358-D6C5-4BBA-903A-1C638FD09FD7Q33186670-2BBFF179-A529-456D-B08F-6441F3F307D6Q33867566-D1B18223-92F0-488F-B48C-D4383081D239Q34354083-635344DB-9D90-4B56-BEC2-14E8715F9178Q34386843-B3F0421D-9E62-41E4-8F22-17A2BB6D2DCEQ34469693-524303B9-4662-4720-934F-67E91F29FEE2Q35104402-809E1336-9476-408A-940B-AC83FEE87167Q35104412-036B25EB-16CA-4473-91B6-4AE7D6340913Q36829195-BA799116-C3D1-4763-985F-36D135D6909BQ36944147-97D63AF2-AAF8-401F-A630-4733C865A3D9Q40313679-2217D61B-DE1A-481B-A244-76A68AC1835FQ40882207-962B617A-535A-4D3A-87DE-652DBAB2386FQ42098634-77E6DE7C-5627-4FD3-9C63-762FB146D031Q43701362-110D7450-D867-4277-9640-D8DA6FE1F443Q43810175-4A3A6593-447B-435B-9531-7A91AF1FE388Q43917521-E879D6C1-D3B8-48EF-B9A6-E3E377B650ABQ44083215-6988C0DF-1C78-4668-8CB5-0613F7846C11Q47780061-38B68E1F-D7A2-4767-B016-57DF21512FB7Q50727408-EED6C00B-1418-40AA-9E47-6860D44F7DFE
P2860
Identification of two amino acids of the human cholecystokinin-A receptor that interact with the N-terminal moiety of cholecystokinin.
description
1997 nî lūn-bûn
@nan
1997 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Identification of two amino ac ...... nal moiety of cholecystokinin.
@ast
Identification of two amino ac ...... nal moiety of cholecystokinin.
@en
Identification of two amino ac ...... nal moiety of cholecystokinin.
@nl
type
label
Identification of two amino ac ...... nal moiety of cholecystokinin.
@ast
Identification of two amino ac ...... nal moiety of cholecystokinin.
@en
Identification of two amino ac ...... nal moiety of cholecystokinin.
@nl
prefLabel
Identification of two amino ac ...... nal moiety of cholecystokinin.
@ast
Identification of two amino ac ...... nal moiety of cholecystokinin.
@en
Identification of two amino ac ...... nal moiety of cholecystokinin.
@nl
P2093
P2860
P356
P1476
Identification of two amino ac ...... inal moiety of cholecystokinin
@en
P2093
C Escrieut
P2860
P304
P356
10.1074/JBC.272.5.2920
P407
P577
1997-01-01T00:00:00Z