1h4l
From Proteopedia
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.
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 Fri May 2 18:25:26 2008
Categories: Homo sapiens | Protein complex | Areces, L. | Dhavan, R. | Musacchio, A. | Peng, J. | Tarricone, C. | Tsai, L H. | Atp-binding | Cdk5 | Cell cycle | Cell division | Cyclin-dependent kinase | Cyclin | P25 | P35 | Phosphorylation | Transferase