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NMR Characterization of Kinase p38 Dynamics in Free and Ligand‐Bound Forms
Author(s) -
Vogtherr Martin,
Saxena Krishna,
Hoelder Swen,
Grimme Susanne,
Betz Marco,
Schieborr Ulrich,
Pescatore Barbara,
Robin Michel,
Delarbre Laure,
Langer Thomas,
Wendt K. Ulrich,
Schwalbe Harald
Publication year - 2006
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.200502770
Subject(s) - chemistry , stereochemistry , motif (music) , structural motif , crystallography , biochemistry , physics , acoustics
In its apo state kinase p38 effects slow motions that can be detected in the NMR spectrum. One of the affected parts is the pharmacologically interesting DFG motif. Diarylurea inhibitors that bind to the DFG‐out conformation lock this motif in a defined state, whereas DFG‐in inhibitors that bind to the adjacent hinge region leave the flexibility of the DFG motif unaffected (see crystal structure of the complex of p38 with the inhibitor SB203580).