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The Binding of Benzoarylsulfonamide Ligands to Human Carbonic Anhydrase is Insensitive to Formal Fluorination of the Ligand
Author(s) -
Lockett Matthew R.,
Lange Heiko,
Breiten Benjamin,
Heroux Annie,
Sherman Woody,
Rappoport Dmitrij,
Yau Patricia O.,
Snyder Philip W.,
Whitesides George M.
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201301813
Subject(s) - binding affinities , ligand (biochemistry) , affinities , carbonic anhydrase , chemistry , binding site , key (lock) , computational biology , carbonic anhydrase ii , computer science , stereochemistry , biochemistry , biology , enzyme , ecology , receptor
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.