1h4l

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spinqualitylabelsall models 1h4l, resolution 2.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

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

Page seeded by OCA on Mon Nov 12 17:12:45 2007