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The Human VPAC1 Receptor
Author(s) -
COUVINEAU ALAIN,
TAN YOSSANVAR,
CERAUDO EMILLE,
LACAPÈRE JEANJACQUES,
MURAIL SAMUEL,
NEUMANN JEANMICHEL,
LABURTHE MARC
Publication year - 2006
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1317.015
Subject(s) - ectodomain , receptor , chemistry , g protein coupled receptor , microbiology and biotechnology , biophysics , biochemistry , biology
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.