1gea
From Proteopedia
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RECEPTOR-BOUND CONFORMATION OF PACAP21
Overview
Many peptide hormones elicit a wide array of physiological effects by, binding to G-protein coupled receptors. We have determined the, conformation of pituitary adenylate cyclase activating polypeptide, PACAP(1--21)NH(2), bound to a PACAP-specific receptor by NMR spectroscopy., Residues 3--7 form a unique beta-coil structure that is preceded by an, N-terminal extended tail. This beta-coil creates a patch of hydrophobic, residues that is important for receptor binding. In contrast, the, C-terminal region (residues 8--21) forms an alpha-helix, similar to that, in the micelle-bound PACAP. Thus, the conformational difference between, PACAP in the receptor-bound and the micelle-bound states is limited to the, N-terminal seven residues. This observation is consistent with the, two-step ligand transportation model in which PACAP first binds to the, membrane nonspecifically and then diffuses two-dimensionally in search of, its receptor; a conformational change at the N-terminal region then allows, specific interactions between the ligand and the receptor.
About this Structure
1GEA is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Conformation of a peptide ligand bound to its G-protein coupled receptor., Inooka H, Ohtaki T, Kitahara O, Ikegami T, Endo S, Kitada C, Ogi K, Onda H, Fujino M, Shirakawa M, Nat Struct Biol. 2001 Feb;8(2):161-5. PMID:11175907
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