1jow
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Crystal structure of a complex of human CDK6 and a viral cyclin
OverviewOverview
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.
About this StructureAbout this Structure
1JOW is a Protein complex structure of sequences from Homo sapiens and Saimiriine herpesvirus 3. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for CDK6 activation by a virus-encoded cyclin., Schulze-Gahmen U, Kim SH, Nat Struct Biol. 2002 Mar;9(3):177-81. PMID:11828325
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