期刊
BIOCHEMICAL JOURNAL
卷 448, 期 -, 页码 417-423出版社
PORTLAND PRESS LTD
DOI: 10.1042/BJ20121513
关键词
cancer; epidermal growth factor receptor (EGFR); erlotinib; gefitinib; inhibitor; molecular dynamics; receptor tyrosine kinase (RTK); X-ray crystallography
资金
- 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
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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