1KXU
CYCLIN H, A POSITIVE REGULATORY SUBUNIT OF CDK ACTIVATING KINASE
Summary for 1KXU
Entry DOI | 10.2210/pdb1kxu/pdb |
Descriptor | CYCLIN H (2 entities in total) |
Functional Keywords | regulatory protein, cyclin, cell cycle, cell division, nuclear protein, alpha-helical structure |
Biological source | Homo sapiens (human) |
Cellular location | Nucleus: P51946 |
Total number of polymer chains | 1 |
Total formula weight | 38886.75 |
Authors | Kim, K.K.,Chamberin, H.M.,Morgan, D.O.,Kim, S.-H. (deposition date: 1996-08-08, release date: 1997-01-27, Last modification date: 2024-02-14) |
Primary citation | Kim, K.K.,Chamberlin, H.M.,Morgan, D.O.,Kim, S.H. Three-dimensional structure of human cyclin H, a positive regulator of the CDK-activating kinase. Nat.Struct.Biol., 3:849-855, 1996 Cited by PubMed 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 A resolution. Cyclin H contains two alpha-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. PubMed: 8836101DOI: 10.1038/nsb1096-849 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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