1u34
From Proteopedia
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3D NMR structure of the first extracellular domain of CRFR-2beta, a type B1 G-protein coupled receptor
Overview
The corticotropin-releasing factor (CRF) ligand family has diverse effects, on the CNS, including the modulation of the stress response. The ligands', effects are mediated by binding to CRF G protein-coupled receptors. We, have determined the 3D NMR structure of the N-terminal extracellular, domain (ECD1) of the mouse CRF receptor 2beta, which is the major ligand, recognition domain, and identified its ligand binding site by, chemical-shift perturbation experiments. The fold is identified as a short, consensus repeat (SCR), a common protein interaction module. Mutagenesis, reveals the integrity of the hormone-binding site in the full-length, receptor. This study proposes that the ECD1 captures the C-terminal, segment of the ligand, whose N terminus then penetrates into the, transmembrane region of the receptor to initiate signaling. Key residues, of SCR in the ECD1 are conserved in the G protein-coupled receptor, subfamily, suggesting the SCR fold in all of the ECD1s of this subfamily.
About this Structure
1U34 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor., Grace CR, Perrin MH, DiGruccio MR, Miller CL, Rivier JE, Vale WW, Riek R, Proc Natl Acad Sci U S A. 2004 Aug 31;101(35):12836-41. Epub 2004 Aug 23. PMID:15326300
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