Dual contacts between peptide agonist ligands and the secretin receptor directly established by photoaffinity labeling

Annals of the New York Academy of Sciences

Volumn 921, Issue , 2000, Pages 381-386

  Dong, Maoqing ^a   Wang, Yan ^a   Miller, Laurence J ^a  

^a MAYO CLINIC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LIGAND; PEPTIDE; SECRETIN;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CONFERENCE PAPER; COVALENT BOND; EXTRACELLULAR SPACE; LIGAND BINDING; PHOTOAFFINITY LABELING; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; STRUCTURE ANALYSIS;

EID: 0034516908     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2000.tb07000.x     Document Type: Conference Paper

References (9)

1. Critical contributions of amino-terminal extracellular domains in agonist binding and activation of secretin and vasoactive intestinal polypeptide receptors. Studies of chimeric receptors
2. Properties of chimeric secretin and VIP receptor proteins indicate the importance of the N-terminal domain for ligand discrimination
3. Multiple extracellular loop domains contribute critical determinants for agonist binding and activation of the secretin receptor
4. Interaction of amino acid residues at positions 8-15 of secretin with the N-terminal domain of the secretin receptor
5. The C-terminus ends of secretin and VIP interact with the N-terminal domains of their receptors
6. Mutational analysis of extracellular cysteine residues of rat secretin receptor shows that disulfide bridges are essential for receptor function
7. 1H-NMR study of the solution conformation of secretin. Resonance assignment and secondary structure
8. Identification of an interaction between residue 6 of the natural peptide ligand and a distinct residue within the amino-terminal tail of the secretin receptor
9. Demonstration of a direct interaction between residue 22 in the carboxyl-terminal half of secretin and the amino-terminal tail of the secretin receptor using photoaffinity labeling