Cited by 1,192Lung Cancer Treatments and MutationsHER2/EGFR in Cancer ResearchProtein Kinase Regulation and GTPase Signaling

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Structures of Lung Cancer-Derived EGFR Mutants and Inhibitor Complexes: Mechanism of Activation and Insights into Differential Inhibitor Sensitivity

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Yun, Cai-Hong, Boggon, Titus J., Li, Yiqun, Woo, Michele S., Greulich, Heidi, Meyerson, Matthew, Eck, Michael J.·2007·Cancer Cell

DOI 10.1016/j.ccr.2006.12.017PMC PMC1939942

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Abstract

Mutations in the EGFR kinase are a cause of non-small-cell lung cancer. To understand their mechanism of activation and effects on drug binding, we studied the kinetics of the L858R and G719S mutants and determined their crystal structures with inhibitors including gefitinib, AEE788, and a staurosporine. We find that the mutations activate the kinase by disrupting autoinhibitory interactions, and that they accelerate catalysis as much as 50-fold in vitro. Structures of inhibitors in complex with both wild-type and mutant kinases reveal similar binding modes for gefitinib and AEE788, but a marked rotation of the staurosporine in the G719S mutant. Strikingly, direct binding measurements show that gefitinib binds 20-fold more tightly to the L858R mutant than to the wild-type enzyme.

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“We also examined binding of the pyrrolopyrimidine compound AEE788 (Novartis Pharmaceuticals), which binds in a manner similar to gefitinib despite the difference in chemical scaffold (8).”
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Authors: Yun, C.-H., Boggon, T. J., Li, Y., Woo, M. S., Greulich, H., Meyerson, M., & Eck, M. J.
Affiliations: Harvard University (US)
Dana-Farber Cancer Institute (US)
Broad Institute (US)
Corresponding author: Eck, Michael J.
ORCID: Yun, Cai-Hong
Boggon, Titus J.
Li, Yiqun
Greulich, Heidi
Meyerson, Matthew
Eck, Michael J.
Venue: Cancer Cell
Publisher: Elsevier BV
Published: 2007-03
Volume: 11
Issue: 3
Pages: 217-227
ISSN: 1535-6108 (ISSN-L)
DOI: 10.1016/j.ccr.2006.12.017
PMC: PMC1939942
OpenAlex: W2111109297
Cited by: 1,192
References: 54
Citations by year: 2026: 58 · 2025: 75 · 2024: 78 · 2023: 84 · 2022: 79 · 2021: 59 · 2020: 72 · 2019: 49 · 2018: 58 · 2017: 57 · 2016: 55 · 2015: 79 · 2014: 63 · 2013: 74 · 2012: 51
FWCI: 40.77
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 2366 d)
Locations: Cancer Cell (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health (CA116020, CA080942)
Leukemia and Lymphoma Society
Topics: Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Lung Cancer Treatments and Mutations
Health Sciences › Medicine › Oncology › HER2/EGFR in Cancer Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Keywords: EGFR, non-small cell lung cancer, EGFR mutation, L858R, kinase activation, gefitinib, AEE788, staurosporine, kinase inhibitor binding, crystal structure, catalytic acceleration, inhibitor sensitivity
MeSH terms: Gefitinib, Lapatinib, Antineoplastic Agents, Binding Sites, Carcinoma, Non-Small-Cell Lung, Enzyme Activation, Humans, Lung Neoplasms, Models, Molecular, Mutation, Protein Conformation, Purines, Quinazolines, Protein Structure, Tertiary, Crystallography, X-Ray, Staurosporine, ErbB Receptors

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Structures of Lung Cancer-Derived EGFR Mutants and Inhibitor Complexes: Mechanism of Activation and Insights into Differential Inhibitor Sensitivity

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