2foq

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{{STRUCTURE_2foq| PDB=2foq | SCENE= }}
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'''Human Carbonic Anhydrase II complexed with two-prong inhibitors'''
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===Human Carbonic Anhydrase II complexed with two-prong inhibitors===
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==Overview==
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The atomic-resolution crystal structures of human carbonic anhydrases I and II complexed with "two-prong" inhibitors are reported. Each inhibitor contains a benzenesulfonamide prong and a cupric iminodiacetate (IDA-Cu(2+)) prong separated by linkers of different lengths and compositions. The ionized NH(-) group of each benzenesulfonamide coordinates to the active site Zn(2+) ion; the IDA-Cu(2+) prong of the tightest-binding inhibitor, BR30, binds to H64 of CAII and H200 of CAI. This work provides the first evidence verifying the structural basis of nanomolar affinity measured for two-prong inhibitors targeting the carbonic anhydrases.
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{{ABSTRACT_PUBMED_16506782}}
==Disease==
==Disease==
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[[Category: Lyase]]
[[Category: Lyase]]
[[Category: Zinc]]
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Revision as of 13:05, 29 July 2008

Image:2foq.png

Template:STRUCTURE 2foq

Contents

Human Carbonic Anhydrase II complexed with two-prong inhibitors

Template:ABSTRACT PUBMED 16506782

Disease

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

About this Structure

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

Reference

Ultrahigh resolution crystal structures of human carbonic anhydrases I and II complexed with "two-prong" inhibitors reveal the molecular basis of high affinity., Jude KM, Banerjee AL, Haldar MK, Manokaran S, Roy B, Mallik S, Srivastava DK, Christianson DW, J Am Chem Soc. 2006 Mar 8;128(9):3011-8. PMID:16506782

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