3FJ5
Crystal structure of the c-src-SH3 domain
Summary for 3FJ5
| Entry DOI | 10.2210/pdb3fj5/pdb |
| Descriptor | Proto-oncogene tyrosine-protein kinase Src, TRIETHYLENE GLYCOL, SULFATE ION, ... (7 entities in total) |
| Functional Keywords | beta shandwich, transferase, atp-binding, kinase, lipoprotein, myristate, nucleotide-binding, phosphoprotein, proto-oncogene, sh2 domain, sh3 domain, tyrosine-protein kinase |
| Biological source | Gallus gallus (Chicken) |
| Cellular location | Cell membrane (By similarity): P00523 |
| Total number of polymer chains | 2 |
| Total formula weight | 13978.31 |
| Authors | Camara-Artigas, A. (deposition date: 2008-12-14, release date: 2009-03-03, Last modification date: 2023-11-01) |
| Primary citation | Morel, B.,Ruiz-Sanz, J.,Luque, I. Intertwined dimeric structure for the SH3 domain of the c-Src tyrosine kinase induced by polyethylene glycol binding Febs Lett., 583:749-753, 2009 Cited by PubMed Abstract: Here we report the first crystal structure of the SH3 domain of the cellular Src tyrosine kinase (c-Src-SH3) domain on its own. In the crystal two molecules of c-Src-SH3 exchange their -RT loops generating an intertwined dimer, in which the two SH3 units, preserving the binding site configuration, are oriented to allow simultaneous binding of two ligand molecules. The dimerization of c-Src-SH3 is induced, both in the crystal and in solution, by the binding of a PEG molecule at the dimer interface, indicating that this type of conformations are energetically close to the native structure. These results have important implications respect to in vivo oligomerization and amyloid aggregation. PubMed: 19185573DOI: 10.1016/j.febslet.2009.01.036 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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