The N-terminal parts of VIP and antagonist PG97-269 physically interact with different regions of the human VPAC1 receptor

Journal of Molecular Neuroscience

Volumn 36, Issue 1-3, 2008, Pages 245-248

  Ceraudo, Emilie ^a   Tan, Yossan Var ^a   Nicole, Pascal ^a   Couvineau, Alain ^a   Laburthe, Marc ^a  

^a INSERM   (France)

Author keywords

GPCR; Photolabeling; VIP; VPAC1 receptor

Indexed keywords

CYANOGEN BROMIDE; PG97 269; UNCLASSIFIED DRUG; VASOACTIVE INTESTINAL POLYPEPTIDE; VASOACTIVE INTESTINAL POLYPEPTIDE ANTAGONIST; VASOACTIVE INTESTINAL POLYPEPTIDE RECEPTOR 1;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; GLYCOSYLATION; NONHUMAN; PHOTOAFFINITY LABELING; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE;

HUMANS; MODELS, MOLECULAR; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; RECEPTORS, VASOACTIVE INTESTINAL POLYPEPTIDE, TYPE I; VASOACTIVE INTESTINAL PEPTIDE;

EID: 58149083478     PISSN: 08958696     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12031-008-9073-7     Document Type: Article

References (11)

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