2cek

CONFORMATIONAL FLEXIBILITY IN THE PERIPHERAL SITE OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE REVEALED BY THE COMPLEX STRUCTURE WITH A BIFUNCTIONAL INHIBITOR

spinqualitylabelsall models 2cek, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2cek is a 1 chain structure with sequence from Torpedo californica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MES, N8T, NAG, NDG, PGE Related: 1acj, 1acl, 1amn, 1ax9, 1cfj, 1dx6, 1e3q, 1e66, 1ea5, 1eea, 1eve, 1fss, 1gpk, 1gpn, 1gqr, 1gqs, 1h22, 1h23, 1hbj, 1jga, 1jgb, 1jjb, 1oce, 1odc, 1qid, 1qie, 1qif, 1qig, 1qih, 1qii, 1qij, 1qik, 1qim, 1qti, 1som, 1u65, 1ut6, 1vot, 1vxo, 1vxr, 1w4l, 1w6r, 1w75, 1w76, 1zgb, 1zgc, 2ace, 2ack, 2c4h, 2c58, 2c5f, 2c5g, 2dfp, 3ace, 4ace Activity: Acetylcholinesterase, with EC number 3.1.1.7 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [ACES_TORCA] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. May be involved in cell-cell interactions. 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 The X-ray crystallographic structure of Torpedo californica acetylcholinesterase (TcAChE) in complex with the bifunctional inhibitor NF595, a potentially new anti-Alzheimer drug, has been solved. For the first time in TcAChE, a major conformational change in the peripheral-site tryptophan residue is observed upon complexation. The observed conformational flexibility highlights the dynamic nature of protein structures and is of importance for structure-based drug design. Conformational flexibility in the peripheral site of Torpedo californica acetylcholinesterase revealed by the complex structure with a bifunctional inhibitor.,Colletier JP, Sanson B, Nachon F, Gabellieri E, Fattorusso C, Campiani G, Weik M J Am Chem Soc. 2006 Apr 12;128(14):4526-7. PMID:16594661 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Torpedo californica acetylcholinesterase with bifunctional inhibitor 3D structures of acetylcholinesterase

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