1w75
From Proteopedia
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|SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Chain+B'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.7 3.1.1.7] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.7 3.1.1.7] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w75 OCA], [http://www.ebi.ac.uk/pdbsum/1w75 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w75 RCSB]</span> | ||
}} | }} | ||
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[[Category: Silman, I.]] | [[Category: Silman, I.]] | ||
[[Category: Sussman, J L.]] | [[Category: Sussman, J L.]] | ||
| - | [[Category: NAG]] | ||
[[Category: alzheimer's disease]] | [[Category: alzheimer's disease]] | ||
[[Category: cholinesterase]] | [[Category: cholinesterase]] | ||
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[[Category: synapse]] | [[Category: synapse]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:32:06 2008'' |
Revision as of 21:32, 30 March 2008
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| , resolution 2.400Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Acetylcholinesterase, with EC number 3.1.1.7 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NATIVE ORTHORHOMBIC FORM OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE (ACHE)
Overview
Bifunctional derivatives of the alkaloid galanthamine, designed to interact with both the active site of the enzyme acetylcholinesterase (AChE) and its peripheral cation binding site, have been assayed with Torpedo californica AChE (TcAChE), and the three-dimensional structures of their complexes with the enzyme have been solved by X-ray crystallography. Differences were noted between the IC(50) values obtained for TcAChE and those for Electrophorus electricus AChE. These differences are ascribed to sequence differences in one or two residues lining the active-site gorge of the enzyme. The binding of one of the inhibitors disrupts the native conformation of one wall of the gorge, formed by the loop Trp279-Phe290. It is proposed that flexibility of this loop may permit the binding of inhibitors such as galanthamine, which are too bulky to penetrate the narrow neck of the gorge formed by Tyr121 and Phe330 as seen in the crystal structure.
About this Structure
1W75 is a Single protein structure of sequence from Torpedo californica. Full crystallographic information is available from OCA.
Reference
The complex of a bivalent derivative of galanthamine with torpedo acetylcholinesterase displays drastic deformation of the active-site gorge: implications for structure-based drug design., Greenblatt HM, Guillou C, Guenard D, Argaman A, Botti S, Badet B, Thal C, Silman I, Sussman JL, J Am Chem Soc. 2004 Dec 1;126(47):15405-11. PMID:15563167
Page seeded by OCA on Mon Mar 31 00:32:06 2008
Categories: Acetylcholinesterase | Single protein | Torpedo californica | Argaman, A. | Botti, S. | Greenblatt, H M. | Silman, I. | Sussman, J L. | Alzheimer's disease | Cholinesterase | Glycoprotein | Gpi-anchor | Hydrolase | Muscle | Nerve | Neurotransmitter degradation | Serine esterase | Serine hydrolase | Signal | Synapse
