1CSK
THE CRYSTAL STRUCTURE OF HUMAN CSKSH3: STRUCTURAL DIVERSITY NEAR THE RT-SRC AND N-SRC LOOP
Summary for 1CSK
| Entry DOI | 10.2210/pdb1csk/pdb |
| Descriptor | C-SRC SH3 DOMAIN (2 entities in total) |
| Functional Keywords | phosphotransferase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm (By similarity): P41240 |
| Total number of polymer chains | 4 |
| Total formula weight | 31407.78 |
| Authors | Mathieu, M.,Wierenga, R.K. (deposition date: 1994-03-22, release date: 1994-07-31, Last modification date: 2024-02-07) |
| Primary citation | Borchert, T.V.,Mathieu, M.,Zeelen, J.P.,Courtneidge, S.A.,Wierenga, R.K. The crystal structure of human CskSH3: structural diversity near the RT-Src and n-Src loop. FEBS Lett., 341:79-85, 1994 Cited by PubMed Abstract: SH3 domains are modules occurring in diverse proteins, ranging from cytoskeletal proteins to signaling proteins, such as tyrosine kinases. The crystal structure of the SH3 domain of Csk (c-Src specific tyrosine kinase) has been refined at a resolution of 2.5 A, with an R-factor of 22.4%. The structure is very similar to the FynSH3 crystal structure. When comparing CskSH3 and FynSH3 it is seen that the structural and charge differences of the RT-Src loop and the n-Src loop, near the conserved Trp47, correlate with different binding properties of these SH3 domains. The structure comparison suggests that those glycines and acid residues which are very well conserved in the SH3 sequences are important for the stability of the SH3 fold. PubMed: 7511113DOI: 10.1016/0014-5793(94)80244-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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