2uz6

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Revision as of 15:41, 29 October 2007

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spinqualitylabelsall models 2uz6, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

ACHBP-TARGETED A-CONOTOXIN CORRELATES DISTINCT BINDING ORIENTATIONS WITH NACHR SUBTYPE SELECTIVITY.

Overview

Neuronal nAChRs are a diverse family of pentameric ion channels with wide, distribution throughout cells of the nervous and immune systems. However, the role of specific subtypes in normal and pathological states remains, poorly understood due to the lack of selective probes. Here, we used a, binding assay based on acetylcholine-binding protein (AChBP), a homolog of, the nicotinic acetylcholine ligand-binding domain, to discover a novel, alpha-conotoxin (alpha-TxIA) in the venom of Conus textile. alpha-TxIA, bound with high affinity to AChBPs from different species and selectively, targeted the alpha(3)beta(2) nAChR subtype. A co-crystal structure of, Ac-AChBP with the enhanced potency analog TxIA(A10L), revealed a 20, degrees backbone tilt compared to other AChBP-conotoxin complexes. ... [(full description)]

About this Structure

2UZ6 is a [Protein complex] structure of sequences from [Aplysia californica] with NAG, NH2 and GOL as [ligands]. Full crystallographic information is available from [OCA].

Reference

AChBP-targeted alpha-conotoxin correlates distinct binding orientations with nAChR subtype selectivity., Dutertre S, Ulens C, Buttner R, Fish A, van Elk R, Kendel Y, Hopping G, Alewood PF, Schroeder C, Nicke A, Smit AB, Sixma TK, Lewis RJ, EMBO J. 2007 Jul 26;. PMID:17660751

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