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Ann N Y Acad Sci. 2006 Jul;1070:205-9.

The human VPAC1 receptor: identification of the N-terminal ectodomain as a major VIP-binding site by photoaffinity labeling and 3D modeling.

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1
INSERM U773, Faculté de Médecine X. Bichat, 16 rue Henri Huchard, 75018 Paris, France. Alain.Couvineau@bichat.inserm.fr

Abstract

The human VPAC1 receptor for VIP and PACAP is a class II Gprotein-coupled receptor (GPCR). The N-terminal ectodomain of the VPAC1 receptor plays a crucial role in VIP binding. Photoaffinity experiments clearly indicated that the 6-28 part of VIP physically interacts with the N-terminal ectodomain. Construction of a 3D model of the N-terminal ectodomain of VPAC1 receptor based on the NMR structure of the mouse CRF receptor 2 indicated the presence of short consensus repeat/Sushi domain. Docking of VIP in the N-terminal ectodomain structural model was performed taking into account the severe constraints provided by photoaffinity. A VIP-binding site was identified on the side of the structured core of the N-terminal ectodomain of the receptor.

PMID:
16888167
DOI:
10.1196/annals.1317.015
[Indexed for MEDLINE]
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