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A Fluorine Scan of Thrombin Inhibitors to Map the Fluorophilicity/Fluorophobicity of an Enzyme Active Site: Evidence for CF⋅⋅⋅CO Interactions
Author(s) -
Olsen Jacob A.,
Banner David W.,
Seiler Paul,
Obst Sander Ulrike,
D'Arcy Allan,
Stihle Martine,
Müller Klaus,
Diederich François
Publication year - 2003
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.200351268
Subject(s) - active site , angstrom , crystallography , molecule , chemistry , crystal structure , fluorine , enzyme , thrombin , x ray , stereochemistry , small molecule , physics , biochemistry , biology , organic chemistry , platelet , quantum mechanics , immunology
A highly fluorophilic environment comprising the HC α CO unit of Asn 98 in the active site of thrombin was identified by X‐ray crystallography of a complex formed between the enzyme and a synthetic inhibitor (see partial X‐ray structure, distances are in Angstroms). Short CF⋅⋅⋅HC α and CF⋅⋅⋅CO contacts involving HC α CO fragments were also frequently observed in small‐molecule X‐ray crystal structures.