1xtn

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(New page: 200px<br /><applet load="1xtn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xtn, resolution 2.20&Aring;" /> '''crystal structure of...)
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[[Image:1xtn.gif|left|200px]]<br /><applet load="1xtn" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1xtn.gif|left|200px]]<br /><applet load="1xtn" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1xtn, resolution 2.20&Aring;" />
caption="1xtn, resolution 2.20&Aring;" />
'''crystal structure of CISK-PX domain with sulfates'''<br />
'''crystal structure of CISK-PX domain with sulfates'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1XTN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XTN OCA].
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1XTN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XTN OCA].
==Reference==
==Reference==
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[[Category: px domain]]
[[Category: px domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:20:12 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:58:34 2008''

Revision as of 13:58, 21 February 2008


1xtn, resolution 2.20Å

Drag the structure with the mouse to rotate

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 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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