Inhibition of the EGF receptor by binding of MIG6 to an activating kinase domain interface

Xuewu Zhang, Kerry A. Pickin, Ron Bose, Natalia Jura, Philip A. Cole and John Kuriyan ()
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Xuewu Zhang: and Howard Hughes Medical Institute, California Institute for Quantitative Sciences, University of California, Berkeley, California 94720, USA
Kerry A. Pickin: Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
Ron Bose: Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
Natalia Jura: and Howard Hughes Medical Institute, California Institute for Quantitative Sciences, University of California, Berkeley, California 94720, USA
Philip A. Cole: Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
John Kuriyan: and Howard Hughes Medical Institute, California Institute for Quantitative Sciences, University of California, Berkeley, California 94720, USA

Nature, 2007, vol. 450, issue 7170, 741-744

Abstract: Crystal structures of complexes between the epidermal growth factor receptor (EGFR) kinase domain and a fragment of its feedback inhibitor MIG6 reveal an allosteric inhibition mechanism. MIG6 binds the cyclin/CDK-like asymmetric dimer interface of EGFR and blocks formation of the activating dimer.

Date: 2007
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DOI: 10.1038/nature05998

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