1i9b

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spinqualitylabelsall models 1i9b, resolution 2.7Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

X-RAY STRUCTURE OF ACETYLCHOLINE BINDING PROTEIN (ACHBP)

Overview

Pentameric ligand gated ion-channels, or Cys-loop receptors, mediate rapid, chemical transmission of signals. This superfamily of allosteric, transmembrane proteins includes the nicotinic acetylcholine (nAChR), serotonin 5-HT3, gamma-aminobutyric-acid (GABAA and GABAC) and glycine, receptors. Biochemical and electrophysiological information on the, prototypic nAChRs is abundant but structural data at atomic resolution, have been missing. Here we present the crystal structure of molluscan, acetylcholine-binding protein (AChBP), a structural and functional, homologue of the amino-terminal ligand-binding domain of an nAChR, alpha-subunit. In the AChBP homopentamer, the protomers have an, immunoglobulin-like topology. Ligand-binding sites are located at each of, five subunit interfaces and contain residues contributed by biochemically, determined 'loops' A to F. The subunit interfaces are highly variable, within the ion-channel family, whereas the conserved residues stabilize, the protomer fold. This AChBP structure is relevant for the development of, drugs against, for example, Alzheimer's disease and nicotine addiction.

About this Structure

1I9B is a Single protein structure of sequence from Lymnaea stagnalis with CA and EPE as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors., Brejc K, van Dijk WJ, Klaassen RV, Schuurmans M, van Der Oost J, Smit AB, Sixma TK, Nature. 2001 May 17;411(6835):269-76. PMID:11357122

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