1odc

STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH N-4'-QUINOLYL-N'-9"-(1",2",3",4" -TETRAHYDROACRIDINYL)-1,8-DIAMINOOCTANE AT 2.2A RESOLUTION

spinqualitylabelsall models 1odc, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1odc 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: A8B, NAG Related: 1zgb, 1amn, 1qti, 1e66, 2j3d, 2vq6, 2ack, 1qii, 2ckm, 1dx6, 1qie, 1qij, 1acl, 1w4l, 2cmf, 2wg0, 1gqs, 2j3q, 1e3q, 2j4f, 1qik, 2dfp, 2c5f, 1ea5, 1eea, 2vjc, 1qif, 2vjb, 1qig, 1zgc, 1qid, 2wfz, 1jjb, 2vjd, 1ut6, 2wg1, 2vt6, 2w9i, 2wg2, 2vt7, 2cek, 1qim, 1gpk, 1jga, 3ace, 1w6r, 1oce, 1som, 1vxo, 2w6c, 2vja, 1cfj, 2v96, 1u65, 1ax9, 1w76, 1h22, 1eve, 2c4h, 2va9, 1gqr, 2ace, 1vxr, 4ace, 2c58, 1hbj, 1vot, 1w75, 2c5g, 1jgb, 2v98, 1gpn, 1qih, 2vb4, 1h23, 1acj, 1fss, 2v97 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 crystal structures were solved for complexes with Torpedo californica acetylcholinesterase of two bivalent tacrine derivative compounds in which the two tacrine rings were separated by 5- and 7-carbon spacers. The derivative with the 7-carbon spacer spans the length of the active-site gorge, making sandwich interactions with aromatic residues both in the catalytic anionic site (Trp84 and Phe330) at the bottom of the gorge and at the peripheral anionic site near its mouth (Tyr70 and Trp279). The derivative with the 5-carbon spacer interacts in a similar manner at the bottom of the gorge, but the shorter tether precludes a sandwich interaction at the peripheral anionic site. Although the upper tacrine group does interact with Trp279, it displaces the phenyl residue of Phe331, thus causing a major rearrangement in the Trp279-Ser291 loop. The ability of this inhibitor to induce large-scale structural changes in the active-site gorge of acetylcholinesterase has significant implications for structure-based drug design because such conformational changes in the target enzyme are difficult to predict and to model. Complexes of alkylene-linked tacrine dimers with Torpedo californica acetylcholinesterase: Binding of Bis5-tacrine produces a dramatic rearrangement in the active-site gorge.,Rydberg EH, Brumshtein B, Greenblatt HM, Wong DM, Shaya D, Williams LD, Carlier PR, Pang YP, Silman I, Sussman JL J Med Chem. 2006 Sep 7;49(18):5491-500. PMID:16942022 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also AChE inhibitors and substrates Acetylcholinesterase complexed with N-9-(1'%2C2'%2C3'%2C4'-tetrahydroacridinyl)-1%2C8-diaminooctane Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (5 carbon linker) Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (7 carbon linker) User:Boris Brumshtein User:Dawn M. Wong 3D structures of acetylcholinesterase

Proteopedia Page Contributors and Editors (what is this?)

OCA