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1h4l
From Proteopedia
STRUCTURE AND REGULATION OF THE CDK5-P25(NCK5A) COMPLEX
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1H4L is a 4 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Tarricone C, Dhavan R, Peng J, Areces LB, Tsai LH, Musacchio A. Structure and regulation of the CDK5-p25(nck5a) complex. Mol Cell. 2001 Sep;8(3):657-69. PMID:11583627
Page seeded by OCA on Mon Feb 16 13:04:15 2009
Categories: Homo sapiens | 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

