2psq
Crystal Structure of Unphosphorylated Unactivated Wild Type FGF Receptor 2 (FGFR2) Kinase Domain
|
OverviewOverview
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, and TIE, are also subject to regulation by this brake. Pathogenic, mutations activate FGFRs and other RTKs by disengaging the brake either, directly or indirectly.
About this StructureAbout this Structure
2PSQ is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Receptor protein-tyrosine kinase, with EC number 2.7.10.1 Full crystallographic information is available from OCA.
ReferenceReference
A molecular brake in the kinase hinge region regulates the activity of receptor tyrosine kinases., Chen H, Ma J, Li W, Eliseenkova AV, Xu C, Neubert TA, Miller WT, Mohammadi M, Mol Cell. 2007 Sep 7;27(5):717-30. PMID:17803937
Page seeded by OCA on Wed Jan 23 13:28:08 2008