1uv6 | pdb_00001uv6

X-RAY STRUCTURE OF ACETYLCHOLINE BINDING PROTEIN (ACHBP) IN COMPLEX WITH CARBAMYLCHOLINE

spinqualitylabelsall models 1uv6, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1uv6 is a 10 chain structure with sequence from Great pond snail. The November 2005 RCSB PDB Molecule of the Month feature on Acetylcholine Receptor by David S. Goodsell is 10.2210/rcsb_pdb/mom_2005_11. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CCE Related: 1i9b, 1uw6, 1ux2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [ACHP_LYMST] Binds to acetylcholine. Modulates neuronal synaptic transmission. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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 ligands. The higher affinity of nicotine is due to a main chain hydrogen bond with the B loop and a closer packing of the aromatic groups. These structures will be useful tools for the development of new drugs involving nicotinic acetylcholine receptor-associated diseases. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Acetylcholine binding protein

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