[HTML][HTML] Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor
J Stamos, MX Sliwkowski, C Eigenbrot - Journal of biological chemistry, 2002 - ASBMB
The crystal structure of the kinase domain from the epidermal growth factor receptor
(EGFRK) including forty amino acids from the carboxyl-terminal tail has been determined to
2.6-Å resolution, both with and without an EGFRK-specific inhibitor currently in Phase III
clinical trials as an anti-cancer agent, erlotinib (OSI-774, CP-358,774, Tarceva TM). The
EGFR family members are distinguished from all other known receptor tyrosine kinases in
possessing constitutive kinase activity without a phosphorylation event within their kinase …
(EGFRK) including forty amino acids from the carboxyl-terminal tail has been determined to
2.6-Å resolution, both with and without an EGFRK-specific inhibitor currently in Phase III
clinical trials as an anti-cancer agent, erlotinib (OSI-774, CP-358,774, Tarceva TM). The
EGFR family members are distinguished from all other known receptor tyrosine kinases in
possessing constitutive kinase activity without a phosphorylation event within their kinase …