1gea: Difference between revisions
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[[Image:1gea.gif|left|200px]] | [[Image:1gea.gif|left|200px]] | ||
'''RECEPTOR-BOUND CONFORMATION OF PACAP21''' | {{Structure | ||
|PDB= 1gea |SIZE=350|CAPTION= <scene name='initialview01'>1gea</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''RECEPTOR-BOUND CONFORMATION OF PACAP21''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1GEA is a [ | 1GEA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GEA OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11175907 11175907] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Endo, S.]] | [[Category: Endo, S.]] | ||
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[[Category: Shirakawa, M.]] | [[Category: Shirakawa, M.]] | ||
[[Category: beta coil]] | [[Category: beta coil]] | ||
[[Category: consecutive beta | [[Category: consecutive beta turn]] | ||
[[Category: helix]] | [[Category: helix]] | ||
[[Category: type-i beta turn]] | [[Category: type-i beta turn]] | ||
[[Category: type-ii beta turn]] | [[Category: type-ii beta turn]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:21:53 2008'' | ||
Revision as of 09:21, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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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