1h4l: Difference between revisions

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[[Image:1h4l.~~gif~~|left|200px]]

[[Image:1h4l.png|left|200px]]

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~~'''~~STRUCTURE AND REGULATION OF THE CDK5-P25(NCK5A) COMPLEX~~'''~~

===STRUCTURE AND REGULATION OF THE CDK5-P25(NCK5A) COMPLEX===

~~==Overview==~~

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~~CDK5 plays an indispensable role in the central nervous system~~, ~~and its deregulation is involved in neurodegeneration. We report the crystal structure of a complex between CDK5 and p25~~, ~~a fragment of~~ the ~~p35 activator. Despite its partial structural similarity with~~ the ~~cyclins, p25 displays an unprecedented mechanism for the regulation of a cyclin-dependent kinase~~. ~~p25 tethers the unphosphorylated T loop of CDK5 in the active conformation~~. ~~Residue Ser159~~, ~~equivalent to Thr160 on CDK2, contributes to the specificity of~~ the ~~CDK5-p35 interaction~~. Its substitution with threonine prevents p35 binding, while the presence of alanine affects neither binding nor kinase activity. Finally, we provide evidence that the CDK5-p25 complex employs a distinct mechanism from the phospho-~~CDK2~~-~~cyclin A complex to establish substrate specificity.~~

The line below this paragraph, {{ABSTRACT_PUBMED_11583627}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11583627 is the PubMed ID number.

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==About this Structure==

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[[Category: Phosphorylation]]

[[Category: Transferase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 18~~:25:26 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:36:59 2008''

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-[[Image:1h4l.gif|left|200px]]
+{{Seed}}
+[[Image:1h4l.png|left|200px]]
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 {{STRUCTURE_1h4l|  PDB=1h4l  |  SCENE=  }}
-'''STRUCTURE AND REGULATION OF THE CDK5-P25(NCK5A) COMPLEX'''
+===STRUCTURE AND REGULATION OF THE CDK5-P25(NCK5A) COMPLEX===
-==Overview==
+<!--
-CDK5 plays an indispensable role in the central nervous system, and its deregulation is involved in neurodegeneration. We report the crystal structure of a complex between CDK5 and p25, a fragment of the p35 activator. Despite its partial structural similarity with the cyclins, p25 displays an unprecedented mechanism for the regulation of a cyclin-dependent kinase. p25 tethers the unphosphorylated T loop of CDK5 in the active conformation. Residue Ser159, equivalent to Thr160 on CDK2, contributes to the specificity of the CDK5-p35 interaction. Its substitution with threonine prevents p35 binding, while the presence of alanine affects neither binding nor kinase activity. Finally, we provide evidence that the CDK5-p25 complex employs a distinct mechanism from the phospho-CDK2-cyclin A complex to establish substrate specificity.
+The line below this paragraph, {{ABSTRACT_PUBMED_11583627}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11583627 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11583627}}
 ==About this Structure==
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 [[Category: Phosphorylation]]
 [[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:25:26 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 06:36:59 2008''