1JOW

Crystal structure of a complex of human CDK6 and a viral cyclin

Summary for 1JOW

• Entry DOI: 10.2210/pdb1jow/pdb
• Related: 1F5Q 1JST
• Descriptor: CYCLIN HOMOLOG, CELL DIVISION PROTEIN KINASE 6 (2 entities in total)
• Functional Keywords: cdk-cyclin complex, cyclin fold, cell cycle-transferase complex, cell cycle/transferase
• Biological source: Saimiriine herpesvirus 2 (Herpesvirus saimiri); More
• Total number of polymer chains: 2
• Total formula weight: 63731.75

Authors

Schulze-Gahmen, U.,Kim, S.H. (deposition date: 2001-07-31, release date: 2002-02-27, Last modification date: 2024-02-07)

Primary citation

Schulze-Gahmen, U.,Kim, S.H.
Structural basis for CDK6 activation by a virus-encoded cyclin.
Nat.Struct.Biol., 9:177-181, 2002

PubMed Abstract: Cyclin from herpesvirus saimiri (Vcyclin) preferentially forms complexes with cyclin-dependent kinase 6 (CDK6) from primate host cells. These complexes show higher kinase activity than host cell CDKs in complex with cellular cyclins and are resistant to cyclin-dependent inhibitory proteins (CDKIs). The crystal structure of human CDK6--Vcyclin in an active state was determined to 3.1 A resolution to better understand the structural basis of CDK6 activation by viral cyclins. The unphosphorylated CDK6 in complex with Vcyclin has many features characteristic of cyclinA-activated, phosphorylated CDK2. There are, however, differences in the conformation at the tip of the T-loop and its interactions with Vcyclin. Residues in the N-terminal extension of Vcyclin wrap around the tip of the CDK6 T-loop and form a short beta-sheet with the T-loop backbone. These interactions lead to a 20% larger buried surface in the CDK6--Vcyclin interface than in the CDK2--cyclinA complex and are probably largely responsible for the specificity of Vcyclin for CDK6 and resistance of the complex to inhibition by INK-type CDKIs.

PubMed: 11828325

Experimental method

X-RAY DIFFRACTION (3.1 Å)