2DQ7
Crystal Structure of Fyn kinase domain complexed with staurosporine
Summary for 2DQ7
| Entry DOI | 10.2210/pdb2dq7/pdb |
| Descriptor | Proto-oncogene tyrosine-protein kinase Fyn, STAUROSPORINE (3 entities in total) |
| Functional Keywords | src family, kinase domain, staurosporine, transferase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: P06241 |
| Total number of polymer chains | 1 |
| Total formula weight | 33111.91 |
| Authors | Kinoshita, T.,Tada, T. (deposition date: 2006-05-23, release date: 2006-07-04, Last modification date: 2024-10-09) |
| Primary citation | Kinoshita, T.,Matsubara, M.,Ishiguro, H.,Okita, K.,Tada, T. Structure of human Fyn kinase domain complexed with staurosporine. Biochem.Biophys.Res.Commun., 346:840-844, 2006 Cited by PubMed Abstract: The tyrosine kinase Fyn is a member of the Src kinase family. Besides the role of Fyn in T cell signal transduction in concert with Lck, its excess activity in the brain is involved with conditions such as Alzheimer's and Parkinson's diseases. Therefore, inhibition of Fyn kinase may help counteract these nervous system disorders. Here, we solved the crystal structure of the human Fyn kinase domain complexed with staurosporine, a potent kinase inhibitor, at 2.8 A resolution. Staurosporine binds to the ATP-binding site of Fyn in a similar manner as in the Lck- and Csk-complexes. The small structural differences in the staurosporine-binding and/or -unbinding region among the three kinase domains may help obtaining the selective inhibitors against the respective kinases. PubMed: 16782058DOI: 10.1016/j.bbrc.2006.05.212 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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