Imatinib binding to human c-Src is coupled to inter-domain allostery and suggests a novel kinase inhibition strategy.

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作者： Yuko,Tsutsui ^[1] ; Daniel,Deredge ^[2] ; Patrick L,Wintrode ^[2] ; Franklin A,Hays ^[1]

作者单位： Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, USA. ^[1] Department of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, Maryland 21201, USA. ^[2] Stephenson Cancer Center, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, USA. ^[3] Harold Hamm Diabetes Center, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, 73104, USA. ^[4]

主题词别构部位(Allosteric Site);抗肿瘤药(Antineoplastic Agents);结合部位(Binding Sites);人类(Humans);配体(Ligands);肽碎片(Peptide Fragments);磷酰化(Phosphorylation);蛋白质结合(Protein Binding);原癌基因蛋白质类pp60(c-src)(Proto-Oncogene Proteins pp60(c-src));src同源域(src Homology Domains)

DOI 10.1038/srep30832

PMID 27480221

发布时间 2018-11-13

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Imatinib binding to human c-Src is coupled to inter-domain allostery and suggests a novel kinase inhibition strategy.

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Imatinib binding to human c-Src is coupled to inter-domain allostery and suggests a novel kinase inhibition strategy.

Scientific reports

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