Detailed Structure of the H2PO4––Guanosine Diphosphate Intermediate in Ras-GAP Decoded from FTIR Experiments by Biomolecular Simulations-Reference-Cited by-同舟云学术

Detailed Structure of the H2PO4––Guanosine Diphosphate Intermediate in Ras-GAP Decoded from FTIR Experiments by Biomolecular Simulations

Published:2012-12-03 Issue:49 Volume:134 Page:20041-20044
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Xia Fei¹,Rudack Till²,Cui Qiang³,Kötting Carsten²,Gerwert Klaus¹²

Affiliation:

1. Chinese Academy of Sciences−Max Planck Partner Institute and Key Laboratory for Computational Biology, Shanghai Institutes for Biological Sciences, 320 Yue Yang Road, Shanghai, 200031, China

2. Department of Biophysics, Ruhr University Bochum, ND 04 North, 44780 Bochum, Germany

3. Department of Chemistry and Theoretical Chemistry Institute, University of Wisconsin, 1101 University Avenue, Madison, Wisconsin 53706, United States

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja310496e

Reference41 articles.

1. Ras-catalyzed hydrolysis of GTP: a new perspective from model studies.

2. The Guanine Nucleotide-Binding Switch in Three Dimensions

3. Structure-Function Relationships of the G Domain, a Canonical Switch Motif

4. Ras and GTPase-activating protein (GAP) drive GTP into a precatalytic state as revealed by combining FTIR and biomolecular simulations

5. Ras history

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