1eou: Difference between revisions

Revision as of 01:22, 1 July 2008

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File:1eou.png

Template:STRUCTURE 1eou

CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH AN ANTICONVULSANT SUGAR SULFAMATECRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH AN ANTICONVULSANT SUGAR SULFAMATE

Template:ABSTRACT PUBMED 11802772

About this StructureAbout this Structure

1EOU is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of human carbonic anhydrase II complexed with an anti-convulsant sugar sulphamate., Recacha R, Costanzo MJ, Maryanoff BE, Chattopadhyay D, Biochem J. 2002 Feb 1;361(Pt 3):437-41. PMID:11802772

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1eou.jpg|left|200px]]
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 {{STRUCTURE_1eou|  PDB=1eou  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH AN ANTICONVULSANT SUGAR SULFAMATE'''
+===CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH AN ANTICONVULSANT SUGAR SULFAMATE===
-==Overview==
+<!--
-The fructose-based sugar sulphamate RWJ-37497, a potent analogue of the widely used anti-epileptic drug topiramate, possesses anti-convulsant and carbonic anhydrase-inhibitory activities. We have studied the binding interactions of RWJ-37497 in the active site of human carbonic anhydrase II by X-ray crystallography. The atomic positions of the enzyme inhibitor complex were refined at a resolution of 2.1 A (1 A=0.1 nm) to the final crystallographic R and R(free) values of 0.18 and 0.23, respectively. The inhibitor co-ordinates to the active-site zinc ion through its oxygen atom and the ionized nitrogen atom of the sulphamate group by replacing the metal-bound water molecules, although the sulphamoyl oxygen atom provides a rather lengthy co-ordination. The 4,5-cyclic sulphate group is positioned in a hydrophobic pocket of the active site, making contacts with the residues Phe-131, Leu-198, Pro-201 and Pro-202. Since the ligand was found to be intact, concerns about RWJ-37947 irreversibly alkylating the enzyme through its 4,5-cyclic sulphate group were dispelled.
+The line below this paragraph, {{ABSTRACT_PUBMED_11802772}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11802772 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11802772}}
 ==About this Structure==
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 [[Category: Hydrolase]]
 [[Category: Protein-inhibitor complex]]
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