1bcd
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(New page: 200px<br /> <applet load="1bcd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bcd, resolution 1.9Å" /> '''X-RAY CRYSTALLOGRAPH...)
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Revision as of 14:02, 12 November 2007
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X-RAY CRYSTALLOGRAPHIC STRUCTURE OF A COMPLEX BETWEEN HUMAN CARBONIC ANHYDRASE II AND A NEW TOPICAL INHIBITOR, TRIFLUOROMETHANE SULPHONAMIDE
Contents |
Overview
It has recently been shown that aliphatic sulphonamides are good, inhibitors of carbonic anhydrase (CA) provided that the pK of the, sulphonamide is low. We have determined the structure of the complex, between CAII and CF3SO2NH2 by X-ray crystallographic methods. The nitrogen, of the sulphonamide is bound to the zinc ion of the enzyme in the usual, manner. The other parts of the inhibitor show a different mode of binding, from aromatic sulphonamides since the trifluoromethyl group is bound at, the hydrophobic part of the active site instead of pointing out from the, active site. It should be possible to design new inhibitors specific for, the different isoenzymes, starting from the present structure.
Disease
Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]
About this Structure
1BCD is a Single protein structure of sequence from Homo sapiens with ZN and FMS as ligands. Active as Carbonate dehydratase, with EC number 4.2.1.1 Full crystallographic information is available from OCA.
Reference
The structure of a complex between carbonic anhydrase II and a new inhibitor, trifluoromethane sulphonamide., Hakansson K, Liljas A, FEBS Lett. 1994 Aug 22;350(2-3):319-22. PMID:8070585
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