1uv6
From Proteopedia
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X-RAY STRUCTURE OF ACETYLCHOLINE BINDING PROTEIN (ACHBP) IN COMPLEX WITH CARBAMYLCHOLINE
Overview
Nicotinic acetylcholine receptors are prototypes for the pharmaceutically, important family of pentameric ligand-gated ion channels. Here we present, atomic resolution structures of nicotine and carbamylcholine binding to, AChBP, a water-soluble homolog of the ligand binding domain of nicotinic, receptors and their family members, GABAA, GABAC, 5HT3 serotonin, and, glycine receptors. Ligand binding is driven by enthalpy and is accompanied, by conformational changes in the ligand binding site. Residues in the, binding site contract around the ligand, with the largest movement in the, C loop. As expected, the binding is characterized by substantial aromatic, and hydrophobic contributions, but additionally there are close contacts, between protein oxygens and positively charged groups in the ... [(full description)]
About this Structure
1UV6 is a [Single protein] structure of sequence from [Lymnaea stagnalis] with CCE as [ligand]. The following page contains interesting information on the relation of 1UV6 with [Acetylcholine Receptor]. Full crystallographic information is available from [OCA].
Reference
Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures., Celie PH, van Rossum-Fikkert SE, van Dijk WJ, Brejc K, Smit AB, Sixma TK, Neuron. 2004 Mar 25;41(6):907-14. PMID:15046723
Page seeded by OCA on Mon Oct 29 20:14:49 2007
