2br8

From Proteopedia

Revision as of 12:19, 30 October 2007

CRYSTAL STRUCTURE OF ACETYLCHOLINE-BINDING PROTEIN (ACHBP) FROM APLYSIA CALIFORNICA IN COMPLEX WITH AN ALPHA-CONOTOXIN PNIA VARIANT

Overview

Conotoxins (Ctx) form a large family of peptide toxins from cone snail, venoms that act on a broad spectrum of ion channels and receptors. The, subgroup alpha-Ctx specifically and selectively binds to subtypes of, nicotinic acetylcholine receptors (nAChRs), which are targets for, treatment of several neurological disorders. Here we present the structure, at a resolution of 2.4 A of alpha-Ctx PnIA (A10L D14K), a potent blocker, of the alpha(7)-nAChR, bound with high affinity to acetylcholine binding, protein (AChBP), the prototype for the ligand-binding domains of the nAChR, superfamily. Alpha-Ctx is buried deep within the ligand-binding site and, interacts with residues on both faces of adjacent subunits. The toxin, itself does not change conformation, but displaces the C loop of AChBP ... [(full description)]

About this Structure

2BR8 is a [Protein complex] structure of sequences from [Aplysia californica] with SO4 and NH2 as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Crystal structure of nicotinic acetylcholine receptor homolog AChBP in complex with an alpha-conotoxin PnIA variant., Celie PH, Kasheverov IE, Mordvintsev DY, Hogg RC, van Nierop P, van Elk R, van Rossum-Fikkert SE, Zhmak MN, Bertrand D, Tsetlin V, Sixma TK, Smit AB, Nat Struct Mol Biol. 2005 Jul;12(7):582-8. Epub 2005 Jun 12. PMID:15951818

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