Residual dipolar couplings as a tool to study molecular recognition of ubiquitin.
RDCs (residual dipolar couplings) in NMR spectroscopy provide information about protein dynamics complementary to NMR relaxation methods, especially in the previously inaccessible time window between the protein correlation time tau(c) and 50 micros. For ubiquitin, new modes of motion of the protein backbone could be detected using RDC-based techniques. An ensemble of ubiquitin based on these RDC values is found to comprise all different conformations that ubiquitin adopts upon binding to different recognition proteins. These conformations in protein-protein complexes had been derived from 46 X-ray structures. Thus, for ubiquitin recognition by other proteins, conformational selection rather than induced fit seems to be the dominant mechanism.
Lakomek
Nils-Alexander
NA
Department for NMR-based Structural Biology, Max-Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Lange
Oliver F
OF
Walter
Korvin F A
KF
Farès
Christophe
C
Egger
Dalia
D
Lunkenheimer
Peter
P
Meiler
Jens
J
Grubmüller
Helmut
H
Becker
Stefan
S
de Groot
Bert L
BL
Griesinger
Christian
C
D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D025801:Ubiquitin / Q000737:chemistry*
D025801:Ubiquitin