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

doi:10.1016/j.molcel.2011.03.004

Cited by 310Protein Kinase Regulation and GTPase SignalingProtein Structure and DynamicsHER2/EGFR in Cancer Research

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

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Jura, Natalia, Zhang, Xuewu, Endres, Nicholas F., Seeliger, Markus A., Schindler, Thomas, Kuriyan, John·2011·Molecular Cell

DOI 10.1016/j.molcel.2011.03.004PMC PMC3175429

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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.

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EGFR mutations are expected to activate EGFR by destabilizing the inactive form of EGFR without ligand stimulation.
“EGFR mutations are expected to activate the EGFR by destabilizing the inactive form of EGFR without ligand stimulation [7–9].”
From In vitro modeling to determine mutation specificity of EGFR tyrosine kinase inhibitors against clinically relevant EGFR mutants in non-small-cell lung cancer (2015) · cites this paper as [8]

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Authors: Jura, N., Zhang, X., Endres, N. F., Seeliger, M. A., Schindler, T., & Kuriyan, J.
Affiliations: QB3 (US)
The University of Texas Southwestern Medical Center (US)
Stony Brook University (US)
F. Hoffmann-La Roche AG (CH)
Corresponding author: Kuriyan, John
ORCID: Jura, Natalia
Zhang, Xuewu
Endres, Nicholas F.
Seeliger, Markus A.
Schindler, Thomas
Kuriyan, John
Venue: Molecular Cell
Publisher: Elsevier BV
Published: 2011-04
Volume: 42
Issue: 1
Pages: 9-22
ISSN: 1097-2765 (ISSN-L)
DOI: 10.1016/j.molcel.2011.03.004
PMC: PMC3175429
OpenAlex: W1992784105
Cited by: 310
References: 104
Citations by year: 2026: 14 · 2025: 18 · 2024: 11 · 2023: 12 · 2022: 17 · 2021: 9 · 2020: 24 · 2019: 17 · 2018: 16 · 2017: 16 · 2016: 20 · 2015: 26 · 2014: 50 · 2013: 27 · 2012: 24
FWCI: 3.19
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 838 d)
Locations: Molecular Cell (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: Howard Hughes Medical Institute
National Cancer Institute (R01CA096504, R01 CA96504-06)
National Institute of General Medical Sciences (R00GM080097)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Health Sciences › Medicine › Oncology › HER2/EGFR in Cancer Research
Keywords: EGF receptor, kinase activation, inactive kinase conformation, kinase domain, cyclin-dependent kinases, Src kinase, alpha-helix stabilization, conformational change
MeSH terms: Allosteric Regulation, Catalysis, Enzyme Activation, Enzyme Stability, Humans, Models, Biological, Models, Molecular, Protein Conformation, Protein Kinases, Protein Structure, Secondary, Protein Structure, Tertiary, Cyclin-Dependent Kinases, src-Family Kinases, Dimerization, Protein Structure, Quaternary, ErbB Receptors

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

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