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| {{STRUCTURE_1jow| PDB=1jow | SCENE= }} | | {{STRUCTURE_1jow| PDB=1jow | SCENE= }} |
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| '''Crystal structure of a complex of human CDK6 and a viral cyclin'''
| | ===Crystal structure of a complex of human CDK6 and a viral cyclin=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11828325}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11828325 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11828325}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Cdk-cyclin complex]] | | [[Category: Cdk-cyclin complex]] |
| [[Category: Cyclin fold]] | | [[Category: Cyclin fold]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:31:48 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:34:30 2008'' |
