2PSQ
Crystal Structure of Unphosphorylated Unactivated Wild Type FGF Receptor 2 (FGFR2) Kinase Domain
Summary for 2PSQ
| Entry DOI | 10.2210/pdb2psq/pdb |
| Related | 1GJO 1OEC 2PVF 2PVY 2PWL 2PY3 2PZ5 2PZP 2PZR 2Q0B |
| Descriptor | Fibroblast growth factor receptor 2, SULFATE ION (3 entities in total) |
| Functional Keywords | kinase domain fold consisting of n- and c-lobes, transferase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cell membrane; Single-pass type I membrane protein. Isoform 14: Secreted. Isoform 19: Secreted: P21802 |
| Total number of polymer chains | 2 |
| Total formula weight | 84660.93 |
| Authors | Chen, H.,Mohammadi, M. (deposition date: 2007-05-07, release date: 2007-09-25, Last modification date: 2023-08-30) |
| Primary citation | Chen, H.,Ma, J.,Li, W.,Eliseenkova, A.V.,Xu, C.,Neubert, T.A.,Miller, W.T.,Mohammadi, M. A molecular brake in the kinase hinge region regulates the activity of receptor tyrosine kinases. Mol.Cell, 27:717-730, 2007 Cited by PubMed Abstract: 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. PubMed: 17803937DOI: 10.1016/j.molcel.2007.06.028 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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