Ontology highlight
ABSTRACT:
SUBMITTER: Chen H
PROVIDER: S-EPMC2094128 | biostudies-literature | 2007 Sep
REPOSITORIES: biostudies-literature
Chen Huaibin H Ma Jinghong J Li Wanqing W Eliseenkova Anna V AV Xu Chongfeng C Neubert Thomas A TA Miller W Todd WT Mohammadi Moosa M
Molecular cell 20070901 5
Activating mutations in the tyrosine kinase domain of receptor tyrosine kinases (RTKs) cause cancer and skeletal disorders. Comparison of the crystal structures of unphosphorylated and phosphorylated wild-type FGFR2 kinase domains with those of seven unphosphorylated pathogenic mutants reveals an autoinhibitory "molecular brake" mediated by a triad of residues in the kinase hinge region of all FGFRs. Structural analysis shows that many other RTKs, including PDGFRs, VEGFRs, KIT, CSF1R, FLT3, TEK, ...[more]