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

Nature Structural Biology

Volumn 3, Issue 10, 1996, Pages 849-855

  Kim, Kyeong Kyu ^a   Chamberlin, Holly M ^b   Morgan, David O ^b   Kim, Sung Hou ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN DEPENDENT KINASE; CYCLINE; TRANSCRIPTION FACTOR;

AMINO ACID SEQUENCE; CELL CYCLE; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME CONFORMATION; ENZYME PHOSPHORYLATION; HUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; REVIEW; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; CLONING, MOLECULAR; CYCLIN-DEPENDENT KINASES; CYCLINS; HUMANS; MOLECULAR SEQUENCE DATA; PROTEIN FOLDING; PROTEIN-SERINE-THREONINE KINASES; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS;

VERTEBRATA;

EID: 0001212842     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb1096-849     Document Type: Review

References (29)

1. Norbury, C. & Nurse, P. Animal cell cycles and their control. Annu. rev. Biochem. 61, 441-470 (1992).
2. Nasmyth, K. Control of the yeast cell cycle by the Cdc28 protein kinase. Curr. opin. Cell Biol. 5, 165-179 (1993).
3. Morgan, D.O. Principles of CDK regulation. Nature 374, 131-134 (1995).
4. Lees, E. Cyclin dependent kinase regulation. Curr. opin. Cell Biol. 7, 773-780 (1995).
5. Fesquet, D. et al. The MO15 gene encodes the catalytic subunit of a protein kinase that activates cdc2 and other cyclin-dependent kinases (CDKs) through phosphorylation of Thr 161 and its homologues. EMBO J. 12, 3111-3121 (1993).
6. Poon, R.Y.C., Yamashita, K., Adamczewski, J.P., Hunt, T. & Shuttleworth, J. The cdc2-related protein p40MO15 is the catalytic subunit of a protein kinase that can activate p33cdk2 and p34cdc2. EMBO J. 12, 3123-3132 (1993).
7. Solomon, M.J., Harper, J.W. & Shuttleworth, J. CAK, the p34 (cdc2) activating kinase, contains a protein identical or closely related to p40 (MO15). EMBO J. 12, 3133-3142 (1993).
8. Fisher, R.P. & Morgan, D.O. A novel cyclin associates with MO15/CDK7 to form the CDK-activating kinase. Cell 78, 713-724 (1994).
9. Makela, T.P. et al. A cyclin associated with the CDK-activating kinase MO15. Nature 371, 254-257 (1994).
10. Fisher, R.P., Jin, P., Chamberlin, H.M. & Morgan, D.O. Alternative mechanisms of CAK assembly require an assembly factor or an activating kinase. Cell 83, 47-57 (1995).
11. Devault, A. et al. MAT1 ('Menage à trois') a new RING finger protein subunit stabilizing cyclin H-CDK7 complexes in starfish and xenopus CAK. EMBO J. 14, 5027-5036 (1995).
12. Tassan, J. P. et al. In vitro assembly of a functional human CDK7-cylin H complex requires MAT1, a novel 36 kDa RING finger protein. EMBO J. 14, 5608-5617 (1995).
13. Roy, R. et. al. The MO15 cell cycle kinase is associated with the TFIIH transcription-DNA repair factor Cell 79, 1093-1101 (1994).
14. Serizawa, H. et al. Association of Cdk-activating kinase subunits with transcription factor TFIIH. Nature 374, 280-282 (1995).
15. Shiekhattar, R. et al. Cdk-activating kinase complex is a component of human transcription factor TFIIH. Nature 374, 283-287 (1995).
16. Jeffrey, P.D. et al. Mechanism of CDK activation revealed by the structure of a cyclin A-CDK2 complex. Nature 376, 313-320 (1995).
17. Brown, N.R. et. al. The crystal structure of cyclin A. Structure 3, 1235-1247 (1995).
18. Nikolov, D.B. et al. Crystal structure of a TFIIB-TBP-TATA-element ternary complex. Nature 377, 119-128 (1995).
19. Bagby, S. et al. Solution structure of the C-terminal core domain of human TFIIB: similarity to cyclin A and interaction with TATA-binding protein. Cell 82, 857-667 (1995).
20. Nugent, J.H.A., Alfa, C.E., Young, T. & Hyams, J.S. Conserved structural motifs in cyclins identified by sequence analysis. J. cell Sci. 99, 669-674 (1991).
21. Jancarik, J. & Kim, S.-H. Sparse matrix sampling: a screening method for crystallization of proteins. J. appl. Crystallogr. 24, 409-411 (1991).
22. Otwinowski, Z., Oscillation data reduction program, in Data collection and Processing (eds. Sawyer, L., Isaacs, N. & Bailey, S.) 56-62 (SERC Daresbury Laboratory, Warrington, England, 1993).
23. Collaborative computing project No. 4 The CCP4 suite: programs for protein crystallography. Acta crystallogr. D50, 760-763 (1994).
24. Cowtan, K.D. Improvement of macromolecular electron-density maps by the simultaneous application of real and reciprocal space constraints. Acta crystallogr. D49, 148-157 (1993).
25. Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta crystallogr. A47, 110-119 (1991).
26. Brünger, A.T. X-PLOR, version 3.1. a system for X-ray crystallography and NMR (Yale Univ. Press, New Haven, CT, 1993).
27. Brünger, A.T. The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475 (1992).
28. Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thronton, J.M. PROCHECK - a program to check the stereochemical quality of protein structures. J. appl. Crystallogr. 26, 283-291 (1993).
29. Kraulis, P.J. MOLSCRIPT - a program to produce both detailed and schematic plots of protein structures. J. appl. Crystallogr. 24, 946-950 (1991).