K-Ras(G12C) inhibitors allosterically control GTP affinity and effector interactions

Jonathan M. Ostrem, Ulf Peters, Martin L. Sos, James A. Wells and Kevan M. Shokat ()
Additional contact information
Jonathan M. Ostrem: Howard Hughes Medical Institute, University of California
Ulf Peters: Howard Hughes Medical Institute, University of California
Martin L. Sos: Howard Hughes Medical Institute, University of California
James A. Wells: University of California
Kevan M. Shokat: Howard Hughes Medical Institute, University of California

Nature, 2013, vol. 503, issue 7477, 548-551

Abstract: Small molecules are developed that irreversibly bind to the common G12C mutant of K-Ras but not the wild-type protein; crystallographic studies reveal the formation of an allosteric pocket that is not apparent in previous Ras studies, and the small molecules shift the affinity of K-Ras to favour GDP over GTP.

Date: 2013
References: Add references at CitEc
Citations: View citations in EconPapers (10)

Downloads: (external link)
https://www.nature.com/articles/nature12796 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:503:y:2013:i:7477:d:10.1038_nature12796

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature12796

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().