2byn
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Upon ligand binding at the subunit interfaces, the extracellular domain of, the nicotinic acetylcholine receptor undergoes conformational changes, and, agonist binding allosterically triggers opening of the ion channel. The, soluble acetylcholine-binding protein (AChBP) from snail has been shown to, be a structural and functional surrogate of the ligand-binding domain, (LBD) of the receptor. Yet, individual AChBP species display disparate, affinities for nicotinic ligands. The crystal structure of AChBP from, Aplysia californica in the apo form reveals a more open loop C and, distinctive positions for other surface loops, compared with previous, structures. Analysis of Aplysia AChBP complexes with nicotinic ligands, shows that loop C, which does not significantly change conformation upon, ... | + | Upon ligand binding at the subunit interfaces, the extracellular domain of, the nicotinic acetylcholine receptor undergoes conformational changes, and, agonist binding allosterically triggers opening of the ion channel. The, soluble acetylcholine-binding protein (AChBP) from snail has been shown to, be a structural and functional surrogate of the ligand-binding domain, (LBD) of the receptor. Yet, individual AChBP species display disparate, affinities for nicotinic ligands. The crystal structure of AChBP from, Aplysia californica in the apo form reveals a more open loop C and, distinctive positions for other surface loops, compared with previous, structures. Analysis of Aplysia AChBP complexes with nicotinic ligands, shows that loop C, which does not significantly change conformation upon, binding of the antagonist, methyllycaconitine, further opens to, accommodate the peptidic antagonist, alpha-conotoxin ImI, but wraps around, the agonists lobeline and epibatidine. The structures also reveal extended, and nonoverlapping interaction surfaces for the two antagonists, outside, the binding loci for agonists. This comprehensive set of structures, reflects a dynamic template for delineating further conformational changes, of the LBD of the nicotinic receptor. |
==About this Structure== | ==About this Structure== | ||
| - | 2BYN is a | + | 2BYN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aplysia_californica Aplysia californica] with NAG, PG4 and 1PE as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BYN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: soluble acetylcholine receptor]] | [[Category: soluble acetylcholine receptor]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:23:30 2007'' |
Revision as of 12:18, 5 November 2007
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CRYSTAL STRUCTURE OF APO ACHBP FROM APLYSIA CALIFORNICA
Overview
Upon ligand binding at the subunit interfaces, the extracellular domain of, the nicotinic acetylcholine receptor undergoes conformational changes, and, agonist binding allosterically triggers opening of the ion channel. The, soluble acetylcholine-binding protein (AChBP) from snail has been shown to, be a structural and functional surrogate of the ligand-binding domain, (LBD) of the receptor. Yet, individual AChBP species display disparate, affinities for nicotinic ligands. The crystal structure of AChBP from, Aplysia californica in the apo form reveals a more open loop C and, distinctive positions for other surface loops, compared with previous, structures. Analysis of Aplysia AChBP complexes with nicotinic ligands, shows that loop C, which does not significantly change conformation upon, binding of the antagonist, methyllycaconitine, further opens to, accommodate the peptidic antagonist, alpha-conotoxin ImI, but wraps around, the agonists lobeline and epibatidine. The structures also reveal extended, and nonoverlapping interaction surfaces for the two antagonists, outside, the binding loci for agonists. This comprehensive set of structures, reflects a dynamic template for delineating further conformational changes, of the LBD of the nicotinic receptor.
About this Structure
2BYN is a Single protein structure of sequence from Aplysia californica with NAG, PG4 and 1PE as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations., Hansen SB, Sulzenbacher G, Huxford T, Marchot P, Taylor P, Bourne Y, EMBO J. 2005 Oct 19;24(20):3635-46. Epub 2005 Sep 29. PMID:16193063
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