Identification of two pairs of spatially approximated residues within the carboxyl terminus of secretin and its receptor.
about
Molecular pharmacology of the secretin receptorSecretin occupies a single protomer of the homodimeric secretin receptor complex: insights from photoaffinity labeling studies using dual sites of covalent attachment.Molecular basis of secretin docking to its intact receptor using multiple photolabile probes distributed throughout the pharmacophoreLigand binding and activation of the secretin receptor, a prototypic family B G protein-coupled receptor.Insights into the impact of phenolic residue incorporation at each position along secretin for receptor binding and biological activitySecretin receptor oligomers form intracellularly during maturation through receptor core domains.Effects of pH and temperature on photoaffinity labeling of Family B G protein-coupled receptors.Spatial approximation between secretin residue five and the third extracellular loop of its receptor provides new insight into the molecular basis of natural agonist binding.Structural and functional insights into the juxtamembranous amino-terminal tail and extracellular loop regions of class B GPCRs.Agonist-dependent dissociation of oligomeric complexes of G protein-coupled cholecystokinin receptors demonstrated in living cells using bioluminescence resonance energy transfer.Paired cysteine mutagenesis to establish the pattern of disulfide bonds in the functional intact secretin receptor.Molecular approximation between a residue in the amino-terminal region of calcitonin and the third extracellular loop of the class B G protein-coupled calcitonin receptor.Importance of the amino terminus in secretin family G protein-coupled receptors. Intrinsic photoaffinity labeling establishes initial docking constraints for the calcitonin receptor.Spatial approximation between two residues in the mid-region of secretin and the amino terminus of its receptor. Incorporation of seven sets of such constraints into a three-dimensional model of the agonist-bound secretin receptor.Spatial proximity between a photolabile residue in position 19 of salmon calcitonin and the amino terminus of the human calcitonin receptor.Use of probes with fluorescence indicator distributed throughout the pharmacophore to examine the peptide agonist-binding environment of the family B G protein-coupled secretin receptor.Fluorescence resonance energy transfer analysis of secretin docking to its receptor: mapping distances between residues distributed throughout the ligand pharmacophore and distinct receptor residues.Spatial approximation between the amino terminus of a peptide agonist and the top of the sixth transmembrane segment of the secretin receptor.
P2860
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P2860
Identification of two pairs of spatially approximated residues within the carboxyl terminus of secretin and its receptor.
description
2000 nî lūn-bûn
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2000年の論文
@ja
2000年学术文章
@wuu
2000年学术文章
@zh-cn
2000年学术文章
@zh-hans
2000年学术文章
@zh-my
2000年学术文章
@zh-sg
2000年學術文章
@yue
2000年學術文章
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2000年學術文章
@zh-hant
name
Identification of two pairs of ...... of secretin and its receptor.
@en
Identification of two pairs of ...... of secretin and its receptor.
@nl
type
label
Identification of two pairs of ...... of secretin and its receptor.
@en
Identification of two pairs of ...... of secretin and its receptor.
@nl
prefLabel
Identification of two pairs of ...... of secretin and its receptor.
@en
Identification of two pairs of ...... of secretin and its receptor.
@nl
P2093
P2860
P356
P1476
Identification of two pairs of ...... of secretin and its receptor.
@en
P2093
P2860
P304
26032-26039
P356
10.1074/JBC.M000612200
P407
P577
2000-08-01T00:00:00Z