Journal
BIOCHEMICAL JOURNAL
Volume 448, Issue -, Pages 417-423Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20121513
Keywords
cancer; epidermal growth factor receptor (EGFR); erlotinib; gefitinib; inhibitor; molecular dynamics; receptor tyrosine kinase (RTK); X-ray crystallography
Categories
Funding
- National Cancer Institute [Y1-CO-1020]
- National Institute of General Medical Sciences [Y1-GM-1104]
- U.S. Department of Energy [DE-AC02-06CH11357]
- National Institutes of Health [R01-CA079992, R01-GM084959]
- National Science Foundation [0835539, 0835389]
- Predoctoral Fellowship from the Great Rivers Affiliate of the American Heart Association [11PRE7670020]
- Directorate For Engineering
- Div Of Chem, Bioeng, Env, & Transp Sys [0853539] Funding Source: National Science Foundation
- Div Of Chem, Bioeng, Env, & Transp Sys
- Directorate For Engineering [0853389] Funding Source: National Science Foundation
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Erlotinib and gefitinib, tyrosine kinase inhibitors used to block EGFR (epidermal growth factor receptor) signalling in cancer, are thought to bind only the active conformation of the EGFR-TKD (tyrosine kinase domain). Through parallel computational and crystallographic studies, we show in the present study that erlotinib also binds the inactive EGFR-TKD conformation, which may have significant implications for its use in EGFR-mutated cancers.
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