2foy: Difference between revisions

Revision as of 08:24, 29 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:2foy.png

Template:STRUCTURE 2foy

Human Carbonic Anhydrase I complexed with a two-prong inhibitorHuman Carbonic Anhydrase I complexed with a two-prong inhibitor

Template:ABSTRACT PUBMED 16506782

About this StructureAbout this Structure

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

ReferenceReference

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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OCA

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-'''Human Carbonic Anhydrase I complexed with a two-prong inhibitor'''
+===Human Carbonic Anhydrase I complexed with a two-prong inhibitor===
-==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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