1XTN
crystal structure of CISK-PX domain with sulfates
Summary for 1XTN
| Entry DOI | 10.2210/pdb1xtn/pdb |
| Related | 1XTE |
| Descriptor | Serine/threonine-protein kinase Sgk3, SULFATE ION (3 entities in total) |
| Functional Keywords | cisk, px domain, transferase |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Cytoplasmic vesicle : Q9ERE3 |
| Total number of polymer chains | 2 |
| Total formula weight | 29109.17 |
| Authors | Xing, Y.,Liu, D.,Zhang, R.,Joachimiak, A.,Songyang, Z.,Xu, W. (deposition date: 2004-10-22, release date: 2004-11-02, Last modification date: 2023-08-23) |
| Primary citation | Xing, Y.,Liu, D.,Zhang, R.,Joachimiak, A.,Songyang, Z.,Xu, W. Structural basis of membrane targeting by the Phox homology domain of cytokine-independent survival kinase (CISK-PX) J.Biol.Chem., 279:30662-30669, 2004 Cited by PubMed Abstract: The cytokine-independent survival kinase (CISK) in the serum and glucocorticoid-regulated kinase family plays an important role in mediating cell growth and survival. N-terminal to its catalytic kinase domain, CISK contains a phox homology (PX) domain, a phosphoinositide-binding motif that directs the membrane localization of CISK and regulates CISK activity. We have determined the crystal structures of the mouse CISK-PX domain to unravel the structural basis of membrane targeting of CISK. In addition to the specific interactions conferred by the phosphoinositide-binding pocket, the structure suggests that a hydrophobic loop region and a hydrophilic beta-turn contribute to the interactions with the membrane. Furthermore, biochemical studies reveal that CISK-PX dimerizes in the presence of the linker between the PX domain and kinase domain, suggesting a multivalent mechanism in membrane localization of CISK. PubMed: 15126499DOI: 10.1074/jbc.M404107200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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