Catalytic Control in the EGF Receptor and Its Connection to General Kinase Regulatory Mechanisms

Natalia Jura, Xuewu Zhang, Nicholas F. Endres, Markus A. Seeliger, Thomas Schindler, John Kuriyan

Research output: Contribution to journalArticle

189 Citations (Scopus)

Abstract

In contrast to the active conformations of protein kinases, which are essentially the same for all kinases, inactive kinase conformations are structurally diverse. Some inactive conformations are, however, observed repeatedly in different kinases, perhaps reflecting an important role in catalysis. In this review, we analyze one of these recurring conformations, first identified in CDK and Src kinases, which turned out to be central to understanding of how kinase domain of the EGF receptor is activated. This mechanism, which involves the stabilization of the active conformation of an α helix, has features in common with mechanisms operative in several other kinases.

Original languageEnglish (US)
Pages (from-to)9-22
Number of pages14
JournalMolecular Cell
Volume42
Issue number1
DOIs
StatePublished - Apr 8 2011

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Epidermal Growth Factor Receptor
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Protein Kinases

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

Catalytic Control in the EGF Receptor and Its Connection to General Kinase Regulatory Mechanisms. / Jura, Natalia; Zhang, Xuewu; Endres, Nicholas F.; Seeliger, Markus A.; Schindler, Thomas; Kuriyan, John.

In: Molecular Cell, Vol. 42, No. 1, 08.04.2011, p. 9-22.

Research output: Contribution to journalArticle

Jura, Natalia ; Zhang, Xuewu ; Endres, Nicholas F. ; Seeliger, Markus A. ; Schindler, Thomas ; Kuriyan, John. / Catalytic Control in the EGF Receptor and Its Connection to General Kinase Regulatory Mechanisms. In: Molecular Cell. 2011 ; Vol. 42, No. 1. pp. 9-22.
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