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  Structure and regulation of the CDK5-p25nck5a complex

Tarricone, C., Dhavan, R., Peng, J., Areces, L. B., Tsai, L.-H., & Musacchio, A. (2001). Structure and regulation of the CDK5-p25nck5a complex. MOLECULAR CELL, 8(3), 657-669. doi:10.1016/S1097-2765(01)00343-4.

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Tarricone, Cataldo1, Author
Dhavan, Rani2, Author
Peng, Junmin2, Author
Areces, Liliana B.1, Author
Tsai, Li-Huei2, Author
Musacchio, Andrea3, Author           
Affiliations:
1Structural Biology Unit, Department of Experimental Oncology, European Institute of Oncology, Via Ripamonti 435, I-20141 Milan, Italy, ou_persistent22              
2Department of Pathology, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115 USA, ou_persistent22              
3Abt. I:Mechanistische Zellbiologie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753287              

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Free keywords: Cataldo Tarricone5, 1, Rani Dhavan5, 2, Junmin Peng2, Liliana B. Areces1, Li-Huei Tsai4, 2, 3, Andrea Musacchio4, 1, Corresponding author contact information 1 Structural Biology Unit, Department of Experimental Oncology, European Institute of Oncology, Via Ripamonti 435, I-20141 Milan, Italy 2 Department of Pathology, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115 USA 3 Howard Hughes Medical Institute, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115 USA
 Abstract: 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.

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 Dates: 2001
 Publication Status: Issued
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Title: MOLECULAR CELL
Source Genre: Journal
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Pages: - Volume / Issue: 8 (3) Sequence Number: - Start / End Page: 657 - 669 Identifier: ISSN: 1097-2765