1xtn
From Proteopedia
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crystal structure of CISK-PX domain with sulfates
Overview
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.
About this Structure
1XTN is a Single protein structure of sequence from Mus musculus with SO4 as ligand. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
Reference
Structural basis of membrane targeting by the Phox homology domain of cytokine-independent survival kinase (CISK-PX)., Xing Y, Liu D, Zhang R, Joachimiak A, Songyang Z, Xu W, J Biol Chem. 2004 Jul 16;279(29):30662-9. Epub 2004 May 4. PMID:15126499
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