Toggle Main Menu Toggle Search

Open Access padlockePrints

The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases

Lookup NU author(s): Professor Martin NobleORCiD, Professor Jane Endicott


Full text for this publication is not currently held within this repository. Alternative links are provided below where available.


Progression through the eukaryotic cell cycle is driven by the orderly activation of cyclin-dependent kinases (CDKs). For activity, CDKs require association with a cyclin and phosphorylation by a separate protein kinase at a conserved threonine residue (T160 in CDK2). Here we present the structure of a complex consisting of phosphorylated CDK2 and cyclin A together with an optimal peptide substrate, HHASPRK. This structure provides an explanation for the specificity of CDK2 towards the proline that follows the phosphorylatable serine of the substrate peptide, and the requirement for the basic residue in the P+3 position of the substrate. We also present the structure of phosphorylated CDK2 plus cyclinA3 in complex with residues 658-668 from the CDK2 substrate p107. These residues include the RXL motif required to target p107 to cyclins. This structure explains the specificity of the RXL motif for cyclins.

Publication metadata

Author(s): Noble MEM; Endicott JA; Brown NR; Johnson LN

Publication type: Article

Publication status: Published

Journal: Nature Cell Biology

Year: 1999

Volume: 1

Issue: 7

Pages: 438-443

Print publication date: 14/10/1999

ISSN (print): 1465-7392

ISSN (electronic): 1476-4679

Publisher: Nature Publishing Group


DOI: 10.1038/15674


Altmetrics provided by Altmetric