Molecular approximations between residues 21 and 23 of secretin and its receptor: development of a model for peptide docking with the amino terminus of the secretin receptor.

Molecular approximations between residues 21 and 23 of secretin and its receptor: development of a model for peptide docking with the amino terminus of the secretin receptor. Research Abstract Details 

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Molecular approximations between residues 21 and 23 of secretin and its receptor: development of a model for peptide docking with the amino terminus of the secretin receptor. Abstract Text:

Maoqing Dong,Polo C-H Lam,Fan Gao,Keiko Hosohata,Delia I Pinon,Patrick M Sexton,Ruben Abagyan,Laurence J Miller,

The structurally unique amino-terminal domain of class II G protein-coupled receptors is critically important for ligand binding and receptor activation. Understanding the precise role it plays requires detailed insights into the molecular basis of its ligand interactions and the conformation of the ligand-receptor complex. In this work, we used two high-affinity, full-agonist, secretin-like photolabile probes having sites for covalent attachment in positions 21 and 23 and used sequential proteolysis and sequencing of the labeled region of the receptor to identify two new spatial approximation constraints. The position 21 probe labeled receptor residue Arg(15), whereas the position 23 probe labeled receptor residue Arg(21). A homology model of the amino-terminal domain of the secretin receptor was developed using the NMR structure of the analogous domain of the corticotropin-releasing factor receptor. This was attached to a homology model of the secretin receptor transmembrane bundle, with the two domains oriented relative to each other based on continuity of the peptide backbone and by imposing a distance restraint recently identified between the amino-terminal WDN sequence and the region of the helical bundle above transmembrane segment six. Secretin was docked to this model using seven sets of spatial approximation constraints identified in previous photoaffinity labeling studies. This model was found to fully accommodate all existing constraints, as well as the two new approximations identified in this work.

Molecular approximations between residues 21 and 23 of secretin and its receptor: development of a model for peptide docking with the amino terminus of the secretin receptor. Publishing Authors By Initials

M Dong,PC Lam,F Gao,K Hosohata,DI Pinon,PM Sexton,R Abagyan,LJ Miller,

For similar hormones, hormone substitutes, and hormone antagonists: hormones: gastrointestinal hormones: secretin research abstracts see: hormones, hormone substitutes, and hormone antagonists: hormones: gastrointestinal hormones: secretin research

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Molecular approximations between residues 21 and 23 of secretin and its receptor: development of a model for peptide docking with the amino terminus of the secretin receptor. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Molecular pharmacology

VOLUME: 72

Page Numbers: 280-90

Journal Abbreviation: Mol. Pharmacol.

ISSN: 0026-895X

DAY: 2

MONTH: 05

YEAR: 2007

Molecular approximations between residues 21 and 23 of secretin and its receptor: development of a model for peptide docking with the amino terminus of the secretin receptor. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 35623

Molecular approximations between residues 21 and 23 of secretin and its receptor: development of a model for peptide docking with the amino terminus of the secretin receptor. Keywords Mesh Terms:

KEYWORDS: Secretin

MESH TERMS: chemistry

Chemical & Substance for Abstract: Molecular approximations between residues 21 and 23 of secretin and its receptor: development of a model for peptide docking with the amino terminus of the secretin receptor. Information

Substance Name: Secretin

Registry Number: 1393-25-5

Grant and Affiliation Information for Molecular approximations between residues 21 and 23 of secretin and its receptor: development of a model for peptide docking with the amino terminus of the secretin receptor.

AFFILIATION: Department of Molecular Pharmacology and Experimental Therapeutics, Mayo Clinic Scottsdale, Scottsdale, Arizona, USA.

Country: United States

AGENCY: United States NIDDK

GRANT: DK46577

ACRONYM: DK

MEDLINETA: Mol Pharmacol

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