2o4z: Difference between revisions

Revision as of 03:09, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2o4z.png

Template:STRUCTURE 2o4z

Crystal structure of the Carbonic Anhydrase II complexed with hydroxysulfamide inhibitorCrystal structure of the Carbonic Anhydrase II complexed with hydroxysulfamide inhibitor

Template:ABSTRACT PUBMED 17346964

About this StructureAbout this Structure

2O4Z is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Carbonic anhydrase inhibitors: the X-ray crystal structure of the adduct of N-hydroxysulfamide with isozyme II explains why this new zinc binding function is effective in the design of potent inhibitors., Temperini C, Winum JY, Montero JL, Scozzafava A, Supuran CT, Bioorg Med Chem Lett. 2007 May 15;17(10):2795-801. Epub 2007 Feb 28. PMID:17346964

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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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-'''Crystal structure of the Carbonic Anhydrase II complexed with hydroxysulfamide inhibitor'''
+===Crystal structure of the Carbonic Anhydrase II complexed with hydroxysulfamide inhibitor===
-==Overview==
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-N-Hydroxysulfamide is a 2000-fold more potent inhibitor of the zinc enzyme carbonic anhydrase (CA, EC 4.2.1.1) as compared to sulfamide. It also inhibits other physiologically relevant isoforms, such as the tumor-associated CA IX and XII (K(I)s in the range of 0.865-1.34microM). In order to understand the binding of this inhibitor to the enzyme active site, the X-ray crystal structure of the human hCA II-N-hydroxysulfamide adduct was resolved. The inhibitor coordinates to the active site zinc ion by the ionized primary amino group, participating in an extended network of hydrogen bonds with amino acid residues Thr199, Thr200 and two water molecules. The additional two hydrogen bonds in which N-hydroxysulfamide bound to hCA II is involved as compared to the corresponding adduct of sulfamide may explain its higher affinity for the enzyme, also providing hints for the design of tight-binding CA inhibitors possessing an organic moiety substituting the NH group in the N-hydroxysulfamide structure.
+The line below this paragraph, {{ABSTRACT_PUBMED_17346964}}, adds the Publication Abstract to the page
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 [[Category: Crystal structure]]
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