Structural similarity between the pocket region of retinoblastoma tumour suppressor and the cyclin-box

Nature Structural Biology

Volumn 4, Issue 5, 1997, Pages 390-395

  Kim, Hye Yeon ^a,b   Cho, Yunje ^a  

^a Korea Institute of Science and Technology   (South Korea)

^b Korea University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; CYCLINE; ONCOPROTEIN; RETINOBLASTOMA PROTEIN; RNA POLYMERASE; TATA BINDING PROTEIN; TRANSCRIPTION FACTOR; VIRUS PROTEIN;

ARTICLE; BINDING SITE; CANCER GENETICS; CELL CYCLE; CRYSTAL STRUCTURE; GENE STRUCTURE; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; RETINOBLASTOMA; TUMOR SUPPRESSOR GENE; X RAY DIFFRACTION;

EID: 0030996584     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0597-390     Document Type: Article

References (40)

1. Weinberg, R. A. The retinoblastoma protein and cell cycle control. Cell 81, 323-330 (1995).
2. Hollingsworth, R. E., Chen, P.-L & Lee, W.-H. Integration of cell cycle control with transcriptional regulation by the retinoblastoma protein. Curr. Opin. Cell Biol. 5, 194-200 (1993).
3. Weinberg, R. A. The retinoblastoma gene and gene product. Cancer Surveys 12, 43-57 (1992).
4. Bookstein, R. et al. Suppression of tumorigenicity of human prostate carcinoma cells by replacing a mutated Rb gene. Science 247, 712-715 (1990).
5. Huang, H. -J. S. et al. Suppression of the neoplastic phenotype by replacement of the Rb gene in human cancer cells. Science 242, 1563-1566 (1988).
6. Dyson, N., Howley, P. M., MŸnger, K. & Harlow, E. The human papilloma virus-16 E7 oncoprotein is able to bind to the retinoblastoma gene product. Science 243, 934-937 (1989).
7. DeCaprio J.A. et al. SV40 large tumor antigen forms a specific complex with the product of the retinoblastoma susceptibility gene. Cell 54, 275-283 (1988).
8. Horowitz, J. M. et al. Point mutational inactivation of the retinoblastoma antioncogene. Science 243, 937-940 (1989).
9. Huang, S. et al. Two distinct and frequently mutated regions of retinoblastoma protein are required for binding to SV40 T antigen. EMBO J. 9, 1815-1822 (1990).
10. Chellappan, S.P., Hiebert, S., Mudryj, M., Horowitz, J.M. & Nevins, J.R. The E2F transcriptional factor is a cellular target for the RB protein. Cell 65, 1053-1061 (1992).
11. Gu, W. et al. Interaction of myogenic factors and the retinoblastoma protein mediates muscle cell commitment and differentiation. Cell 72, 309-324 (1993)
12. White, R. J. et al. Repression of RNA polymerase III transcription by the retinoblastoma protein. Nature 382, 88-90 (1996).
13. Cavanaugh, A. H. et al. Activity of RNA polymerase I transcription factor UBF blocked by Rb gene product. Nature 374, 177-180 (1995).
14. Kouarides, T. Transcriptional control by the retinioblastoma protein. Semin.Cancer Biol. 6, 91-98 (1995).
15. Hagemeier, C., Bannister, A. J., Cook, A. & Kouzarides, T. The activation domain of transcription factor PU.1 binds the retinoblastoma (RB) protein and the transcription factor TFIID in vitro: RB shows sequence similarity to TFIID and TFIIB. Proc. Natn. Acad. Sci.USA 90, 1580-1584 (1993).
16. Brown, N. R. et al. The crystal structure of Cyclin A. Structure 3, 1235-1247 (1995).
17. Jeffrey, P. D. et al. Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex. Nature 376, 313-320 (1995).
18. 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, 857-867 (1995).
19. Nikolov, D. B. et al. Crystal strucutre of a TFIIB-TBP-TATA element ternary complex. Nature 377, 119-128 (1995).
20. Ewen, M. B., Xing, Y., Lawrence, J. B. & Livingston, D. M. Molecular cloning, chromosomal mapping, and expression of the cDNA for p107, a retinoblastoma gene product-related protein. Cell 66, 1155-1164 (1991).
21. Li, Y. et al. The adenovirus E1A-associated p130-kD protein is encoded by a member of the retinoblastoma gene family and physically interacts with cyclins A and E. Genes Dev. 7, 2366-2377 (1993).
22. Stirdivant, S. M., Ahern, J. D., Oliff, A. & Heimbrook, D. C. Retinoblastoma protein binding properties are dependent on 4 cysteine residues in the protein binding pocket. J. Biol. Chem. 267, 14846-14851 (1992).
23. Gibson, T. J., Thomson, J. D., Blocker, A. & Kouzarides, T. Evidence for a protein domain superfamily shared by the cyclins, TFIIB and RB/p107. Nucleic Acids Res. 22, 946-952 (1994).
24. Jones, D.T., Taylor, W.R. & Thornton, J. M. A new approach to protein fold recognition. Nature 358, 86-89 (1992).
25. Hensey, C. E., et al. Identification of discrete structural domains in the retinoblastoma protein. J. Biol. Chem. 269, 1380-1387 (1994).
26. Chow, K. N. B & Dean, D. C. Domain A and B in the Rb pocket interact to form a transcriptional repressor motif. Mol. Cell. Biol. 16, 4862-4868 (1996).
27. Lees, J.A., Buchkovich, K.J., Marshak, D.R., Anderson. C.W. & Harlow, E. The retinoblastoma protein is phosphorylated on multiple sites byhuman cdc2. EMBO J. 10, 4279-4290 (1991).
28. Knudson, E.S. & Wang, J.Y.J. Differential regulation of retinoblastoma protein function by specific phosphorylation sites. J. Biol. Chem. 271, 8313-8320 (1996).
29. Russo, A. A., Jeffery, P. D. & Pavletich, N. P. Structural basis of cyclin-dependent kinase activation by phosphorylation. Nature Struct. Biol. 3, 696-700 (1996).
30. Kaelin, W. G., Palas, D.C., DeCaprio, J.A., Kaye, F.J. & Livingston, D. M. Identification of cellular proteins that can interact specifically with the T/E1A-binding region of the retinoblastoma gene product. Cell 64, 521-532.
31. Collaborative Computational Project Number 4. The CCP4 Suite: Program for protein crystallography. Acta Crystallogr. D50, 760-763 (1994)
32. Zhang, K.Y.G. SQUASH-Combining constraints for macromolecular phase refinement and extension.Acta Crystallogr. D49, 213-222 (1993).
33. Jones, T.A., Zou, J.-Y., & Cowan, S.W. Improved methods of building protein models in electron density maps and the location errors in these models. Acta Crystallogr. A47, 110-119 (1991).
34. Sack, J.S. CHAIN: a crystallographic modelling program. J. molec. Graphics, 6, 224-225 (1988).
35. Brünger, A. T. X-PLOR, a system for crystallography and NMR, Version 3.1 (Yale Univ. Press, New Haven, CT, 1992)
36. Tronrud, D. E., Ten Eyck, L. F. & Matthews, B. W. An efficient general purpose Least-Squares Refinement Program for Macromolecular Structures.Acta Crystallogr. A43, 489-501 (1987).
37. Merrit, E. A. & Murphy, M. E. P. Raster 3D Version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr. D50, 869-873 (1994).
38. Kabsch, W. & Sander, C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22, 2577-2637 (1983).
39. Kraulis, P. J. Molscript: a program to produce both detailed and schematic plots of protein structures. J. appl. Crystallogr. 24, 946-950 (1991).
40. Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insight from the interfacial and thermodynamic properties of hydrocarbons. Proteins:Structure, Function and Genetics, 11, 281-296 (1991).