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1h4l

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(New page: 200px<br /> <applet load="1h4l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h4l, resolution 2.65&Aring;" /> '''STRUCTURE AND REGUL...)
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Revision as of 15:06, 12 November 2007

Image:1h4l.gif

1h4l, resolution 2.65Å

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

Contents

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.

Disease

Known diseases associated with this structure: Microcephaly, primary autosomal recessive, 3 OMIM:[608201]

About this Structure

1H4L is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure and regulation of the CDK5-p25(nck5a) complex., Tarricone C, Dhavan R, Peng J, Areces LB, Tsai LH, Musacchio A, Mol Cell. 2001 Sep;8(3):657-69. PMID:11583627

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