Crystal structure of the PAC1R extracellular domain unifies a consensus fold for hormone recognition by class B G-protein coupled receptors

PLoS ONE

Volumn 6, Issue 5, 2011, Pages

  Kumar, Shiva ^a,b   Pioszak, Augen ^a,c   Zhang, Chenghai ^a   Swaminathan, Kunchithapadam ^b   Xu, H Eric ^a  

^a VAN ANDEL RESEARCH INSTITUTE   (United States)

^b NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^c UNIVERSITY OF OKLAHOMA COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HYPOPHYSIS ADENYLATE CYCLASE ACTIVATING POLYPEPTIDE; HYPOPHYSIS ADENYLATE CYCLASE ACTIVATING POLYPEPTIDE RECEPTOR 1; ADCYAP1 PROTEIN, HUMAN; CYCLIC AMP; G PROTEIN COUPLED RECEPTOR; HORMONE;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; HORMONE RECEPTOR INTERACTION; MOLECULAR RECOGNITION; PROTEIN DOMAIN; PROTEIN FOLDING; CHEMISTRY; CONSENSUS SEQUENCE; EXTRACELLULAR MATRIX; HUMAN; METABOLISM; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; X RAY CRYSTALLOGRAPHY;

CONSENSUS SEQUENCE; CRYSTALLOGRAPHY, X-RAY; CYCLIC AMP; EXTRACELLULAR MATRIX; HORMONES; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; PITUITARY ADENYLATE CYCLASE-ACTIVATING POLYPEPTIDE; PROTEIN CONFORMATION; PROTEIN FOLDING; RECEPTORS, G-PROTEIN-COUPLED; RECEPTORS, PITUITARY ADENYLATE CYCLASE-ACTIVATING POLYPEPTIDE, TYPE I;

EID: 79956281483     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0019682     Document Type: Article

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