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Three-dimensional structure of human cyclin H, a positive regulator of the CDK-activating kinase

Nature Structural Biology volume 3, pages 849–855 (1996)Cite this article

Abstract

Cyclin-dependent kinases (CDKs), which play a key role in cell cycle control, are activated by the CDK activating kinase (CAK), which activates cyclin-bound CDKs by phosphorylation at a specific threonine residue. Vertebrate CAK contains two key components: a kinase subunit with homology to its substrate CDKs and a regulatory subunit with homology to cyclins. We have determined the X-ray crystal structure of the regulatory subunit of CAK, cyclin H, at 2.6 Å resolution. Cyclin H contains two α-helical core domains with a fold similar to that of cyclin A, a regulatory subunit of CAK substrate CDK2, and of TFIIB, a transcription factor. Outside of the core domains, the N- and C-terminal regions of the three structures are completely different. The conformational differences between cyclin H and A structures may reflect functional differences between the two cyclins.

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Authors and Affiliations

  1. Department of Chemistry and Earnest Orlando Lawrence Berkeley National Laboratory, University of California, Berkeley, California, 94720, USA

    Kyeong Kyu Kim & Sung-Hou Kim

  2. Department of Physiology, University of California, San Francisco, California, 94143-0444, USA

    Holly M. Chamberlin & David O. Morgan

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  1. Kyeong Kyu Kim
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  2. Holly M. Chamberlin
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  4. Sung-Hou Kim
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Kim, K., Chamberlin, H., Morgan, D. et al. Three-dimensional structure of human cyclin H, a positive regulator of the CDK-activating kinase. Nat Struct Mol Biol 3, 849–855 (1996). https://doi.org/10.1038/nsb1096-849

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