Cited by 42Enzyme function and inhibitionEnzyme Structure and FunctionBiochemical and Molecular Research

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The structure of a complex between carbonic anhydrase II and a new inhibitor, trifluoromethane sulphonamide

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Håkansson, K., Liljas, A.·1994·FEBS Letters

Abstract

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.

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  1. 1984 Clarendon Press Oxford J.W. Pflugrath M.A. Saper F.A. Quicho S. Hall T. Ashida Methods in Applied Crystallography and Computing 404 407

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Metadata

Authors
Håkansson, K., & Liljas, A.
Affiliations
Lund University (SE)
Corresponding author
Liljas, A.
Venue
FEBS Letters
Publisher
Wiley
Published
1994-08-22
Volume
350
Issue
2-3
Pages
319-322
ISSN
  • 0014-5793 (ISSN-L)
  • 1873-3468
OpenAlex
W2020999457
Cited by
36
References
29
Citations by year
2021: 3 · 2018: 1 · 2015: 1 · 2014: 2 · 2012: 2
FWCI
1.27
Type
journal article
Language
en
Open access
Locations
  • FEBS Letters (publishedVersion)
  • PubMed (publishedVersion)
Funders
Knut och Alice Wallenbergs Stiftelse
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme function and inhibition
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
Keywords
carbonic anhydrase II, enzyme-inhibitor complex, zinc binding, hydrophobic binding, active site, inhibitor design, isozymes
MeSH terms
Binding Sites, Carbonic Anhydrases, Carbonic Anhydrase Inhibitors, Chlorofluorocarbons, Methane, Humans, Models, Molecular, Sulfonamides, Crystallography, X-Ray

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