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The structure of a complex between carbonic anhydrase II and a new inhibitor, trifluoromethane sulphonamide
Author(s) -
Håkansson K.,
Liljas A.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00798-5
Subject(s) - carbonic anhydrase , chemistry , sulfonamide , active site , enzyme , carbonic anhydrase ii , trifluoromethyl , stereochemistry , zinc , medicinal chemistry , biochemistry , organic chemistry , alkyl
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 CF 3 SO 2 NH 2 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.