Conformational States of Ras Complexed with the GTP Analogue GppNHp or GppCH2p: Implications for the Interaction with Effector Proteins-Reference-Cited by-同舟云学术

Conformational States of Ras Complexed with the GTP Analogue GppNHp or GppCH2p: Implications for the Interaction with Effector Proteins

Published:2005-01-25 Issue:6 Volume:44 Page:2225-2236
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Spoerner Michael¹,Nuehs Andrea¹,Ganser Petra¹,Herrmann Christian¹,Wittinghofer Alfred¹,Kalbitzer Hans Robert¹

Affiliation:

1. Institut für Biophysik und physikalische Biochemie, Universität Regensburg, Universitätsstrasse 31, 93053 Regensburg, Germany, and Abteilung Strukturelle Biologie, Max-Planck-Institut für molekulare Physiologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi0488000

Reference42 articles.

1. Geyer, M., Schweins, T., Herrmann, C., Prisner, T., Wittinghofer, A., and Kalbitzer, H. R. (1996) Conformational transitions in p21 2236 (Ras) and in its complexes with the effector protein Raf-RBD and the GTPase,Biochemistry35, 10308−10320.

2. Observation of Slow Dynamic Exchange Processes in Ras Protein Crystals by 31P Solid State NMR Spectroscopy

3. Bellew, B. F., Halkides, C. J., Gerfen, G. J., Griffin, R. G., and Singel, D. J. (1996) High frequency (139.5 GHz) electron paramagnetic resonance characterization of Mn(II)-H2(17)O interactions in GDP and GTP forms of p21 ras,Biochemistry35, 12186−12193.

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