Tumor suppressor INK4: Comparisons of conformational properties between p16(INK4A) and p18(INK4C)

Journal of Molecular Biology

Volumn 294, Issue 1, 1999, Pages 201-211

  Yuan, Chunhua ^a   Li, Junan ^a   Selby, Thomas L ^a   Byeon, In Ja L ^a   Tsai, Ming Daw ^a  

^a OHIO STATE UNIVERSITY   (United States)

Author keywords

Conformational flexibility of INK4 proteins; Conformational stability of INK4 proteins; p15(INK4B); p16(INK4A); p18(INK4C)

Indexed keywords

ANKYRIN; CYCLIN DEPENDENT KINASE INHIBITOR; INHIBITOR PROTEIN; PROTEIN P16;

ARTICLE; HUMAN; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STABILITY; THERMODYNAMICS;

EID: 0033585104     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3231     Document Type: Article

References (35)

1. Abragam A. Principles of Nuclear Magnetism. 1961;Clarendon Press, Oxford.
2. Bai Y., Milne J. S., Mayne L., Englander S. W. Primary structure effects on peptide group hydrogen exchange. Proteins: Struct. Funct. Genet. 17:1993;75-86.
3. Bai Y., Milne J. S., Mayne L., Englander S. W. Protein stability parameters measured by hydrogen exchange. Proteins: Struct. Funct. Genet. 20:1994;4-14.
4. INK4a. Structure. 6:1998;1279-1290.
5. Boice J. A., Fairman R. Structural characterization of the tumor-suppressor p16, an ankyrin-like repeat protein. Protein Sci. 5:1996;1776-1784.
6. INK4A: determination of solution structure and analyses of its interaction with cyclin-dependent kinase 4. Mol. Cell. 1:1998;421-431.
7. Clarke J., Fersht A. R. Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation. Biochemistry. 32:1993;4322-4329.
8. Clarke J., Itzhaki L. S. Hydrogen exchange and protein folding. Curr. Opin. Struct. Biol. 8:1998;112-118.
9. Englander S. W., Kallenbach N. R. Hydrogen exchange and structural dynamics of protein and nucleic acids. Quart. Rev. Biophys. 16:1984;521-655.
10. 2O in protein NMR. Application to sensitivity enhancement and NOE measurements. J. Am. Chem. Soc. 115:1993;12593-12594.
11. INK4d. FEBS Letters. 401:1997;127-132.
12. 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. Biochemistry. 28:1989;8972-8979.
13. INK4C. Biochemistry. 38:1999;2930-2940.
14. Lipari G., Szabo A. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J. Am. Chem. Soc. 104:1982a;4546-4559.
15. Lipari G., Szabo A. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results. J. Am. Chem. Soc. 104:1982b;4559-4570.
16. INK4d. Nature. 389:1997;999-1003.
17. INK4a. Nature Struct. Biol. 5:1998;85-88.
18. Muchmore D. C., McIntosh L. P., Russel C. B., Anderson D. E., Dahlquist F. W. Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance. Methods Enzymol. 177:1989;44-73.
19. Mullins L. S., Pace C. N., Raushel F. M. Conformational stability of ribonuclease T1 determined by hydrogen-deuterium exchange. Protein Sci. 6:1997;1387-1395.
20. Myers J. K., Pace C. N., Scholtz J. M. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4:1995;2138-2148.
21. Nozaki Y. The preparation of guanidine hydrochloride. Methods Enzymol. 26:1972;43-50.
22. Pace C. N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131:1986;266-279.
23. Palmer A. G. Probing molecular motion by NMR. Curr. Opin. Struct. Biol. 7:1997;732-737.
24. 15N NMR relaxation experiments at two field strengths. J. Mol. Biol. 283:1998;221-229.
25. INK4a. Nature. 395:1998;237-243.
26. Sedgwick S. G., Smerdon S. J. The ankyrin repeat: a diversity of interactions on a common structural framework. Trends Biochem. Sci. 24:1999;311-316.
27. Serrano M., Hannon G. J., Beach D. A new regulatory motif in cell-cycle control causing specific inhibition of cyclin D/CDK4. Nature. 366:1993;704-707.
28. Sherr C. J. Cancer cell cycles. Science. 274:1996;1672-1677.
29. Swint-Kruse L., Robertson A. D. Temperature and pH dependences of hydrogen exchange and global stability for ovomucoid third domain. Biochemistry. 35:1996;171-180.
30. Tang K. S., Guralnick B. L., Wang W. K., Fersht A. R., Itzhaki L. S. Stability and folding of the tumor suppressor protein p16. J. Mol. Biol. 285:1999;1869-1886.
31. INK4A: structural characterization of wild-type and mutant proteins by NMR and circular dichroism. Biochemistry. 35:1996;9475-9487.
32. 1NK4 mutations. Nature Struct. Biol. 5:1998;74-81.
33. Wagner G. Prospects for NMR of large proteins. J. Biomol. NMR. 3:1993;375-385.
34. Woodward C. K., Hilton B. D. Hydrogen isotope exchange kinetics; of single protons in BPTI. Biophys. J. 32:1980;561-575.
35. INK4 proteins encoded by tumor-derived alleles. J. Biol. Chem. 271:1996;28734-28737.