2geh

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Revision as of 20:11, 12 November 2007

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spinqualitylabelsall models 2geh, resolution 2.0Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

N-Hydroxyurea, a versatile zinc binding function in the design of metalloenzyme inhibitors

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

N-Hydroxyurea binds both to carbonic anhydrase (CA) and to matrix, metalloproteinases (MMPs). X-ray crystallography showed N-hydroxyurea to, bind in a bidentate mode by means of the oxygen and nitrogen atoms of the, NHOH moiety to the Zn(II) ion of CA, participating in a network of, hydrogen bonds with a water molecule and Thr199. A derivatized, N-hydroxyurea showed low-micromolar affinity for several CAs. This simple, zinc binding function may be exploited for obtaining potent metalloenzyme, inhibitors, due to its versatility of binding to the metal ion present in, the active site of such enzymes.

Disease

Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]

About this Structure

2GEH is a Single protein structure of sequence from Homo sapiens with ZN, HG and NHY as ligands. Active as Carbonate dehydratase, with EC number 4.2.1.1 Full crystallographic information is available from OCA.

Reference

N-hydroxyurea--a versatile zinc binding function in the design of metalloenzyme inhibitors., Temperini C, Innocenti A, Scozzafava A, Supuran CT, Bioorg Med Chem Lett. 2006 Aug 15;16(16):4316-20. Epub 2006 Jun 12. PMID:16759856

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