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

Ostrem, Jonathan M; Peters, Ulf; Sos, Martin L; Wells, James A; Shokat, Kevan M

Ostrem, Jonathan M; Peters, Ulf; Sos, Martin L; Wells, James A; Shokat, Kevan M.

Affiliation

Ostrem JM; 1] Department of Cellular and Molecular Pharmacology, Howard Hughes Medical Institute, University of California, San Francisco, California 94158, USA [2].

Nature ; 503(7477): 548-51, 2013 Nov 28.

Article in En | MEDLINE | ID: mdl-24256730

Subject(s)

Allosteric Site/drug effects; Guanosine Diphosphate/metabolism; Guanosine Triphosphate/metabolism; Mutant Proteins/antagonists & inhibitors; Mutant Proteins/metabolism; Oncogene Protein p21(ras)/antagonists & inhibitors; Oncogene Protein p21(ras)/metabolism; Allosteric Regulation/drug effects; Apoptosis/drug effects; Cell Line, Tumor; Crystallography, X-Ray; Cysteine/genetics; Cysteine/metabolism; Drug Discovery; Genes, ras/genetics; Humans; Lung Neoplasms/drug therapy; Lung Neoplasms/metabolism; Lung Neoplasms/pathology; Models, Molecular; Mutant Proteins/genetics; Oncogene Protein p21(ras)/genetics; Static Electricity; Substrate Specificity; raf Kinases/metabolism

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Oncogene Protein p21(ras) / Allosteric Site / Mutant Proteins / Guanosine Diphosphate / Guanosine Triphosphate Limits: Humans Language: En Journal: Nature Year: 2013 Type: Article

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