The Binding of Benzoarylsulfonamide Ligands to Human Carbonic Anhydrase is Insensitive to Formal Fluorination of the Ligand1. Issue 30 (20th June 2013)

• Record Type: Journal Article
• Authors: Lockett, Matthew R.; Lange, Heiko; Breiten, Benjamin; Heroux, Annie; Sherman, Woody; Rappoport, Dmitrij; Yau, Patricia O.; Snyder, Philip W.; Whitesides, George M.
• Is Part Of: Angewandte Chemie international edition. Volume 52:Issue 30(2013)
• Page Start: 7714
• Page End: 7717
• Publication Date: 2013-06-20
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201301813
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>It's the water that matters</bold>. Pairs of benzo‐ and perfluorobenzoarylsulfonamide ligands bind to human carbonic anhydrase with a conserved binding geometry, an enthalpy‐driven binding, and indistinguishable binding affinities (see picture). These data support the pervasive theory that the lock‐and‐key model disregards an important component of binding: the water, which fills the binding pocket of the protein and surrounds the ligand.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg270w4gnn" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>