2c9t

From Proteopedia

Revision as of 10:58, 30 October 2007

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

Overview

The nicotinic acetylcholine receptor (nAChR) is the prototype member of, the superfamily of pentameric ligand-gated ion channels. How the, extracellular ligand-binding domain coordinates selective binding of, ligand molecules to different subtypes of the receptor is unknown at the, structural level. Here, we present the 2.2-A crystal structure of a, homolog of the ligand-binding domain of the nAChR, Aplysia californica, AChBP (Ac-AChBP), in complex with alpha-conotoxin ImI. This conotoxin is, unique in its selectivity toward the neuronal alpha3beta2 and alpha7, nAChR, a feature that is reflected in its selective binding to Ac-AChBP, compared with other AChBP homologs. We observe a network of interactions, between the residues of the ligand-binding site and the toxin, in which, ImI Arg-7 ... [(full description)]

About this Structure

2C9T is a [Protein complex] structure of sequences from [Aplysia californica] and [Conus imperialis] with NH2 as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Structural determinants of selective alpha-conotoxin binding to a nicotinic acetylcholine receptor homolog AChBP., Ulens C, Hogg RC, Celie PH, Bertrand D, Tsetlin V, Smit AB, Sixma TK, Proc Natl Acad Sci U S A. 2006 Mar 7;103(10):3615-20. Epub 2006 Feb 27. PMID:16505382

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