2geh

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{{STRUCTURE_2geh| PDB=2geh | SCENE= }}
{{STRUCTURE_2geh| PDB=2geh | SCENE= }}
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'''N-Hydroxyurea, a versatile zinc binding function in the design of metalloenzyme inhibitors'''
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===N-Hydroxyurea, a versatile zinc binding function in the design of metalloenzyme inhibitors===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_16759856}}
==About this Structure==
==About this Structure==
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[[Category: Crystal structure]]
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[[Category: Inhibitor]]
[[Category: Inhibitor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:00:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:14:51 2008''

Revision as of 02:14, 28 July 2008

Image:2geh.png

Template:STRUCTURE 2geh

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

Template:ABSTRACT PUBMED 16759856

About this Structure

2GEH is a Single protein structure of sequence from Homo sapiens. 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

Page seeded by OCA on Mon Jul 28 05:14:51 2008

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