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Angew Chem Int Ed Engl. 2013 Jul 22;52(30):7714-7. doi: 10.1002/anie.201301813. Epub 2013 Jun 20.

The binding of benzoarylsulfonamide ligands to human carbonic anhydrase is insensitive to formal fluorination of the ligand.

Author information

1
Department of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, MA 02138, USA.

Abstract

It's the water that matters. 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.

KEYWORDS:

biomolecular recognition; carbonic anhydrase; hydrophobic effect; protein-ligand binding; water

PMID:
23788494
DOI:
10.1002/anie.201301813
[Indexed for MEDLINE]

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