Photoaffinity labeling demonstrates physical contact between vasoactive intestinal peptide and the N-terminal ectodomain of the human VPAC1 receptor.
about
VPAC receptors: structure, molecular pharmacology and interaction with accessory proteinsTransmembrane signal transduction by peptide hormones via family B G protein-coupled receptorsIdentification of specific calcitonin-like receptor residues important for calcitonin gene-related peptide high affinity binding.The vasoactive intestinal peptide (VIP) alpha-Helix up to C terminus interacts with the N-terminal ectodomain of the human VIP/Pituitary adenylate cyclase-activating peptide 1 receptor: photoaffinity, molecular modeling, and dynamicsDetermining the environment of the ligand binding pocket of the human angiotensin II type I (hAT1) receptor using the methionine proximity assay.Targeting VIP and PACAP receptor signalling: new therapeutic strategies in multiple sclerosis.Mechanisms of ligand binding to the parathyroid hormone (PTH)/PTH-related protein receptor: selectivity of a modified PTH(1-15) radioligand for GalphaS-coupled receptor conformationsThe VPAC1 receptor: structure and function of a class B GPCR prototype.Structural and functional insights into the juxtamembranous amino-terminal tail and extracellular loop regions of class B GPCRs.Novel parathyroid hormone (PTH) antagonists that bind to the juxtamembrane portion of the PTH/PTH-related protein receptor.Importance of the amino terminus in secretin family G protein-coupled receptors. Intrinsic photoaffinity labeling establishes initial docking constraints for the calcitonin receptor.Photolabelling the urotensin II receptor reveals distinct agonist- and partial-agonist-binding sites.Chemical synthesis and characterization of silver-protected vasoactive intestinal peptide nanoparticles.Spatial proximity between a photolabile residue in position 19 of salmon calcitonin and the amino terminus of the human calcitonin receptor.Diffuse pharmacophoric domains of vasoactive intestinal peptide (VIP) and further insights into the interaction of VIP with the N-terminal ectodomain of human VPAC1 receptor by photoaffinity labeling with [Bpa6]-VIP.Peptide agonist docking in the N-terminal ectodomain of a class II G protein-coupled receptor, the VPAC1 receptor. Photoaffinity, NMR, and molecular modeling.
P2860
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P2860
Photoaffinity labeling demonstrates physical contact between vasoactive intestinal peptide and the N-terminal ectodomain of the human VPAC1 receptor.
description
2003 nî lūn-bûn
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2003年の論文
@ja
2003年学术文章
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2003年学术文章
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2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
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2003年學術文章
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name
Photoaffinity labeling demonst ...... n of the human VPAC1 receptor.
@en
Photoaffinity labeling demonst ...... n of the human VPAC1 receptor.
@nl
type
label
Photoaffinity labeling demonst ...... n of the human VPAC1 receptor.
@en
Photoaffinity labeling demonst ...... n of the human VPAC1 receptor.
@nl
prefLabel
Photoaffinity labeling demonst ...... n of the human VPAC1 receptor.
@en
Photoaffinity labeling demonst ...... n of the human VPAC1 receptor.
@nl
P2093
P2860
P356
P1476
Photoaffinity labeling demonst ...... n of the human VPAC1 receptor.
@en
P2093
Alain Couvineau
Jean Van Rampelbergh
Marc Laburthe
Yossan-Var Tan
P2860
P304
36531-36536
P356
10.1074/JBC.M304770200
P407
P577
2003-06-13T00:00:00Z