NDLI: Docking of Linear Peptide Antagonists into the Human V1a Vasopressin Receptor IDENTIFICATION OF BINDING DOMAINS BY PHOTOAFFINITY LABELING

Content Provider	Journal of Biological Chemistry (JBC)
Author	Phalipou, Sylvie Seyer, René Cotte, Nathalie Breton, Christophe Barberis, Claude Hibert, Marcel Mouillac, Bernard
Abstract	A novel photoactivatable linear peptide antagonist selective for the V1a vasopressin receptor, [125I][Lys(3N3 Phpa)8]HO-LVA, was synthesized, characterized, and used to photolabel the human receptor expressed in Chinese hamster ovary cells. Two specific glycosylated protein species at 85–90 and 46 kDa were covalently labeled, a result identical to that obtained with a previous photosensitive ligand, [125I]3N3Phpa-LVA (Phalipou, S., Cotte, N., Carnazzi, E., Seyer, R., Mahe, E., Jard, S., Barberis, C., and Mouillac, B. (1997) J. Biol. Chem.272, 26536–26544). To identify contact sites between the new photoreactive analogue and the V1a receptor, the labeled receptors were digested with Lys-C or Asp-N endoproteinases and chemically cleaved with CNBr. Fragmentation with CNBr, Lyc-C, and Asp-N used alone or in combination, led to the identification of a restricted receptor region spanning the first extracellular loop. The results established that sequence Asp112–Pro120 could be considered as the smallest covalently labeled fragment with [125I][Lys(3N3Phpa)8]HO-LVA. Based on the present experimental result and on previous photoaffinity labeling data obtained with [125I]3N3Phpa-LVA (covalent attachment to transmembrane domain VII), three-dimensional models of the antagonist-bound receptors were constructed and then verified by site-directed mutagenesis studies. Strikingly, these two linear peptide antagonists, when bound to the V1a receptor, could adopt a pseudocyclic conformation similar to that of the cyclic agonists. Despite divergent functional properties, these peptide antagonists could interact with a transmembrane-binding site significantly overlapping that of the natural hormone vasopressin.
Related Links	http://www.jbc.org/content/274/33/23316.abstract
Ending Page	23327
Starting Page	23316
Page Count	12
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	33
Volume Number	274
DOI	10.1074/jbc.274.33.23316
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	1999-08-13
Access Restriction	Open
Subject Keyword	Arginine-vasopressin (AVP) Chinese hamster ovary (CHO) Oxytocin (OT) Transmembrane region (TMR) 3-azidophenylpropionyl1-DTyr(Me)2-Phe3-Gln4-Asn5-Arg6-Pro7-Arg8-Tyr9-NH2 (3N3Phpa-LVA) 4-hydroxyphenylacetyl1-DTyr(Me)2-Phe3-Gln4-Asn5-Arg6-Pro7-Arg8-NH2 (HO-LVA) High performance liquid chromatography (HPLC) Phosphate-buffered saline (PBS) Inositol phosphate (IP) Polyacrylamide gel electrophoresis (PAGE) N-[2-hydroxy-1,1-bis(hydroxymethyl)ethyl]glycine (Tricine) (benzotriazolyloxy)tripyrrolidinophosphonium hexafluorophosphate (PyBOP) PROTEIN CHEMISTRY AND STRUCTURE 4-hydroxyphenylpropionyl1-DTyr(Me)2-Phe3-Gln4-Asn5-Arg6-Pro7-Lys(3-azidophenylpropionyl)8-NH2 ([Lys(3N3Phpa)8]HO-LVA)
Alternative Title	Docking of Linear Peptide Antagonists into the Human V1a Vasopressin Receptor
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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