This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1xtn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(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...)
Line 1: Line 1:
-
[[Image:1xtn.gif|left|200px]]<br /><applet load="1xtn" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[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==
-
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.
+
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==
-
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].
+
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==
Line 25: Line 25:
[[Category: px domain]]
[[Category: px domain]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:20:12 2007''
+
''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

Page seeded by OCA on Thu Feb 21 15:58:34 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools