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A monkey wrench in the kinase machine

Nature Structural & Molecular Biology volume 14, pages 11201121 (2007) | Download Citation

Last year Zhang, Kuriyan and colleagues demonstrated that an asymmetric dimer interaction between EGF receptor kinase domains is a key element of receptor activation. They now show that a cellular protein that inhibits receptor activity targets this dimer interface, not only uncovering an important regulatory mechanism but also opening a new route to therapeutic kinase inhibition.

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Affiliations

  1. Daniel J. Leahy is in the Department of Biophysics & Biophysical Chemistry, Johns Hopkins University School of Medicine, 725 N. Wolfe St., Baltimore, Maryland 21205, USA. dleahy@jhmi.edu

    • Daniel J Leahy

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DOI

https://doi.org/10.1038/nsmb1207-1120

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