1YI5

Crystal structure of the a-cobratoxin-AChBP complex

Summary for 1YI5

• Entry DOI: 10.2210/pdb1yi5/pdb
• Related: 1I9B 1UV6 1UW6 1UX2
• Descriptor: Acetylcholine-binding protein, Long neurotoxin 1 (2 entities in total)
• Functional Keywords: acetylcholine binding protein, snake three-fingered alpha-neurotoxin, toxin
• Biological source: Lymnaea stagnalis (great pond snail); More
• Cellular location: Secreted: P58154 P01391
• Total number of polymer chains: 10
• Total formula weight: 158523.09

Authors

Bourne, Y.,Talley, T.T.,Hansen, S.B.,Taylor, P.,Marchot, P. (deposition date: 2005-01-11, release date: 2005-05-17, Last modification date: 2024-10-30)

Primary citation

Bourne, Y.,Talley, T.T.,Hansen, S.B.,Taylor, P.,Marchot, P.
Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake alpha-neurotoxins and nicotinic receptors
Embo J., 24:1512-1522, 2005

PubMed Abstract: 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.

PubMed: 15791209
DOI: 10.1038/sj.emboj.7600620

Experimental method

X-RAY DIFFRACTION (4.2 Å)