2byq
CRYSTAL STRUCTURE OF APLYSIA CALIFORNICA ACHBP IN COMPLEX WITH EPIBATIDINE
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OverviewOverview
The crystal structure of the snake long alpha-neurotoxin, alpha-cobratoxin, bound to the pentameric acetylcholine-binding protein, (AChBP) from Lymnaea stagnalis, was solved from good quality density maps, despite a 4.2 A overall resolution. The structure unambiguously reveals, the positions and orientations of all five three-fingered toxin molecules, inserted at the AChBP subunit interfaces and the conformational changes, associated with toxin binding. AChBP loops C and F that border the, ligand-binding pocket move markedly from their original positions to wrap, around the tips of the toxin first and second fingers and part of its, C-terminus, while rearrangements also occur in the toxin fingers. At the, interface of the complex, major interactions involve aromatic and, aliphatic side ... [(full description)]
About this StructureAbout this Structure
2BYQ is a [Single protein] structure of sequence from [Aplysia californica] with EPJ as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake alpha-neurotoxins and nicotinic receptors., Bourne Y, Talley TT, Hansen SB, Taylor P, Marchot P, EMBO J. 2005 Apr 20;24(8):1512-22. Epub 2005 Mar 24. PMID:15791209
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