2byq
From Proteopedia
| Line 5: | Line 5: | ||
==Overview== | ==Overview== | ||
| - | 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 .. | + | 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 chains within the AChBP binding pocket and, at the buried, tip of the toxin second finger, conserved Phe and Arg residues that, partially mimic a bound agonist molecule. Hence this structure, in, revealing a distinctive and unpredicted conformation of the toxin-bound, AChBP molecule, provides a lead template resembling a resting state, conformation of the nicotinic receptor and for understanding selectivity, of curaremimetic alpha-neurotoxins for the various receptor species. |
==About this Structure== | ==About this Structure== | ||
| - | 2BYQ is a | + | 2BYQ 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 EPJ as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BYQ OCA]. |
==Reference== | ==Reference== | ||
| Line 27: | Line 27: | ||
[[Category: receptor]] | [[Category: 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 14:23:49 2007'' |
Revision as of 12:18, 5 November 2007
|
CRYSTAL STRUCTURE OF APLYSIA CALIFORNICA ACHBP IN COMPLEX WITH EPIBATIDINE
Overview
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 chains within the AChBP binding pocket and, at the buried, tip of the toxin second finger, conserved Phe and Arg residues that, partially mimic a bound agonist molecule. Hence this structure, in, revealing a distinctive and unpredicted conformation of the toxin-bound, AChBP molecule, provides a lead template resembling a resting state, conformation of the nicotinic receptor and for understanding selectivity, of curaremimetic alpha-neurotoxins for the various receptor species.
About 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.
Reference
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
Page seeded by OCA on Mon Nov 5 14:23:49 2007
