1bcd: Difference between revisions

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==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.

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==

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[[Category: lyase(oxo-acid)]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 15~~:31:46 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:53:46 2008''

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 23: / Line 23: @@
 [[Category: lyase(oxo-acid)]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:31:46 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:53:46 2008''