1F5Q

CRYSTAL STRUCTURE OF MURINE GAMMA HERPESVIRUS CYCLIN COMPLEXED TO HUMAN CYCLIN DEPENDENT KINASE 2

Summary for 1F5Q

• Entry DOI: 10.2210/pdb1f5q/pdb
• Descriptor: CYCLIN DEPENDENT KINASE 2, GAMMA HERPESVIRUS CYCLIN, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: herpesviral cyclin, cyclin dependent kinase. protein-protein complex, transferase
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 126123.63

Authors

Card, G.L.,Knowles, P.,Laman, H.,Jones, N.,McDonald, N.Q. (deposition date: 2000-06-15, release date: 2000-12-27, Last modification date: 2024-02-07)

Primary citation

Card, G.L.,Knowles, P.,Laman, H.,Jones, N.,McDonald, N.Q.
Crystal structure of a gamma-herpesvirus cyclin-cdk complex.
EMBO J., 19:2877-2888, 2000

PubMed Abstract: Several gamma-herpesviruses encode proteins related to the mammalian cyclins, regulatory subunits of cyclin-dependent kinases (cdks) essential for cell cycle progression. We report a 2.5 A crystal structure of a full-length oncogenic viral cyclin from gamma-herpesvirus 68 complexed with cdk2. The viral cyclin binds cdk2 with an orientation different from cyclin A and makes several novel interactions at the interface, yet it activates cdk2 by triggering conformational changes similar to cyclin A. Sequences within the viral cyclin N-terminus lock part of the cdk2 T-loop within the core of the complex. These sequences and others are conserved amongst the viral and cellular D-type cyclins, suggesting that this structure has wider implications for other cyclin-cdk complexes. The observed resistance of this viral cyclin-cdk complex to inhibition by the p27(KIP:) cdk inhibitor is explained by sequence and conformational variation in the cyclin rendering the p27(KIP:)-binding site on the cyclin subunit non-functional.

PubMed: 10856233
DOI: 10.1093/emboj/19.12.2877

Experimental method

X-RAY DIFFRACTION (2.5 Å)