1QMZ

PHOSPHORYLATED CDK2-CYCLYIN A-SUBSTRATE PEPTIDE COMPLEX

Summary for 1QMZ

• Entry DOI: 10.2210/pdb1qmz/pdb
• Related: 1FIN 1JST 1JSU
• Descriptor: CELL DIVISION PROTEIN KINASE 2, G2/MITOTIC-SPECIFIC CYCLIN A, SUBSTRATE PEPTIDE, ... (6 entities in total)
• Functional Keywords: cell cycle, complex (protein kinase-cyclin), cyclin, cdk, phosphorylation, substrate complex
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Nucleus: P20248
• Total number of polymer chains: 6
• Total formula weight: 130528.79

Authors

Brown, N.R.,Noble, M.E.M.,Endicott, J.A.,Johnson, L.N. (deposition date: 1999-10-11, release date: 1999-12-14, Last modification date: 2024-10-16)

Primary citation

Brown, N.R.,Noble, M.E.,Endicott, J.A.,Johnson, L.N.
The Structural Basis for Specificity of Substrate and Recruitment Peptides for Cyclin-Dependent Kinases
Nat.Cell Biol., 1:438-, 1999

PubMed Abstract: 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 cyclin A3 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.

PubMed: 10559988
DOI: 10.1038/15674

Experimental method

X-RAY DIFFRACTION (2.2 Å)