1l4w
From Proteopedia
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NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin
Overview
The structure of a peptide corresponding to residues 182-202 of the, acetylcholine receptor alpha1 subunit in complex with alpha-bungarotoxin, was solved using NMR spectroscopy. The peptide contains the complete, sequence of the major determinant of AChR involved in alpha-bungarotoxin, binding. One face of the long beta hairpin formed by the AChR peptide, consists of exposed nonconserved residues, which interact extensively with, the toxin. Mutations of these receptor residues confer resistance to the, toxin. Conserved AChR residues form the opposite face of the beta hairpin, which creates the inner and partially hidden pocket for acetylcholine. An, NMR-derived model for the receptor complex with two alpha-bungarotoxin, molecules shows that this pocket is occupied by the conserved, alpha-neurotoxin residue R36, which forms cation-pi interactions with both, alphaW149 and gammaW55/deltaW57 of the receptor and mimics acetylcholine.
About this Structure
1L4W is a Protein complex structure of sequences from Bungarus multicinctus. Full crystallographic information is available from OCA.
Reference
The mechanism for acetylcholine receptor inhibition by alpha-neurotoxins and species-specific resistance to alpha-bungarotoxin revealed by NMR., Samson A, Scherf T, Eisenstein M, Chill J, Anglister J, Neuron. 2002 Jul 18;35(2):319-32. PMID:12160749
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