2Q0B: Crystal Structure Of Fgf Receptor 2 (fgfr2) Kinase Domain Harboring The Pathogenic E565a Mutation Responsible For Pfeiffer Syndrome

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.
PDB ID: 2Q0BDownload
MMDB ID: 59356
PDB Deposition Date: 2007/5/21
Updated in MMDB: 2016/12
Experimental Method:
x-ray diffraction
Resolution: 2.9  Å
Source Organism:
Similar Structures:
Biological Unit for 2Q0B: dimeric; determined by author
Molecular Components in 2Q0B
Label Count Molecule
Proteins (2 molecules)
Fibroblast Growth Factor Receptor 2(Gene symbol: FGFR2)
Molecule annotation
Chemicals (6 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB