Urea-dependent unfolding of HIV-1 protease studied by circular dichroism and small-angle X-ray scattering

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1794, Issue 1, 2009, Pages 70-74

  Kogo, Hiroyuki ^a   Takeuchi, Kayoko ^a   Inoue, Hideshi ^a   Kihara, Hiroshi ^b   Kojima, Masaki ^a   Takahashi, Kenji ^a  

^a TOKYO UNIVERSITY OF PHARMACY AND LIFE SCIENCES   (Japan)

^b KANSAI MEDICAL UNIVERSITY   (Japan)

Author keywords

CD; HIV 1 protease; SAXS; Two state transition; Unfolding

Indexed keywords

PEPSIN A; PROTEINASE; UREA;

ARTICLE; CIRCULAR DICHROISM; ENZYME ACTIVITY; ENZYME STRUCTURE; HUMAN IMMUNODEFICIENCY VIRUS 1; MOLECULAR SIZE; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

CIRCULAR DICHROISM; HIV PROTEASE; PEPSIN A; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SCATTERING, SMALL ANGLE; UREA; X-RAY DIFFRACTION;

HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 56449121015     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.09.022     Document Type: Article

References (26)

1. Wong-Staal F., and Gallo R.C. Human T-lymphotropic retroviruses. Nature 317 (1985) 395-403
2. Navia M.A., Fitzgerald P.M.D., Mckeever B.M., Leu C.-T., Heimbach J.C., Herber W.K., Sigal I.S., Darke P.L., and Springer J.P. Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1. Nature 337 (1989) 615-620
3. Wlodawer A., Miller M., Jaskólski M., Sathyanarayana B.K., Baldwin E., Weber I.T., Selk L.M., Clawson L., Schneider J., and Kent S.B.H. Conserved folding in retroviral protease: crystal structure of a synthetic HIV-1 protease. Science 245 (1989) 616-621
4. Rao J.K., Erickson J.W., and Wlodawer A. Structural and evolutionary relationships between retroviral and eucaryotic proteinases. Biochemistry 30 (1991) 4663-4671
5. Dorsey B.D., Levin R.B., McDaniel S.L., Vacca J.P., Guare J.P., Darke P.L., Zugay J.A., Emini E.A., Schleif W.A., Quintero J.C., Lin J.H., Chen I.-W., Holloway M.K., Fitzgerald P.M.D., Axel M.G., Ostovic D., Anderson P.S., and Huff J.R. L-735, 524: the design of a potent and orally bioavailable HIV protease inhibitor. J. Med. Chem. 37 (1994) 3443-3451
6. Condra J.H., Schleif W.A., Blahy O.M., Gabryelski L.J., Graham D.J., Quintero J.C., Rhodes A., Robbins H.L., Roth E., Shivaprakash M., Titus D., Yang T., Teppler H., Squires K.E., Deutsch P.J., and Emini E.A. In vivo emergence of HIV-1 variants resistant to multiple protease inhibitors. Nature 374 (1995) 569-571
7. Tang J., James M.N.G., Hsu I.N., Jenkins J.A., and Blundell T.L. Structural evidence for gene duplication in the evolution of the acid proteases. Nature 271 (1978) 618-621
8. Boggetto N., and Reboud-Ravaux M. Dimerization inhibitors of HIV-1 protease. Biol. Chem. 383 (2002) 1321-1324
9. Grant S.K., Deckman I.C., Culp J.S., Minnich M.D., Brooks I.S., Hensley P., Debouck C., and Meek T.D. Use of protein unfolding studies to determine the conformational and dimeric stabilities of HIV-1 and SIV proteases. Biochemistry 31 (1992) 9491-9501 HHIV
10. Ishima R., Ghirlando R., Tözsér J., Gronenborn A.M., Torchia D.A., and Louis J.M. Folded monomer of HIV-1 protease. J. Biol. Chem. 276 (2001) 49110-49116
11. Xie D., Gulnik S., Gustchina E., Yu B., Shao W., Qoronfleh W., Nathan A., and Erickson J.W. Drug resistance mutations can affect dimer stability of HIV-1 protease at neutral pH. Protein Sci. 8 (1999) 1702-1707
12. Ido E., Han H., Kezdy F., and Tang J. Kinetic studies of human immunodeficiency virus type 1 protease and its active-site hydrogen bond mutant A28S. J. Biol. Chem. 266 (1991) 24359-24366
13. Polgar L., Szeltner Z., and Boros I. Substrate-dependent mechanisms in the catalysis of human immunodeficiency virus protease. Biochemistry 33 (1994) 9351-9357
14. Ito K., Kamikubo H., Yagi N., and Amemiya Y. Correction method and software for image distortion and nonuniform response in charge-coupled device-based x-ray detectors utilizing x-ray image intensifier. Jpn. J. Appl. Phys. 44 (2005) 8684-8691
15. Semisotnov G., Kihara H., Kotova N.V., Kimura K., Amemiya Y., Wakabayashi K., Serdyuk I.N., Timchenko A.A., Chiba K., Nikaido K., Ikura T., and Kuwajima K. Protein globularization during folding. A study by synchrotron small-angle x-ray scattering. J. Mol. Biol. 262 (1996) 559-574
16. Glatter O., and Kratky O. Small-Angle X-ray Scattering (1982), Academic Press, New York
17. Kojima M., Tanokura M., Maeda M., Kimura K., Amemiya Y., Kihara H., and Takahashi K. pH-dependent unfolding of aspergillopepsin II studied by small-angle x-ray scattering. Biochemistry 39 (2000) 1364-1372
18. Darke P.L., Leu C.-T.L., Davis L.J., Heimbach J.C., Diehl R.E., Hill W.S., Dixon R.A.F., and Sigal I.S. Human immunodeficiency virus protease. Bacterial expression and characterization of the purified aspartic protease. J. Biol. Chem. 264 (1989) 2307-2312
19. 6-85. Protein Sci. 15 (2006) 2596-2604
20. Flory P.J. Principles of Polymer Chemistry (1953), Cornell Univeristy Press, Ithaca, NY
21. Kohn J.E., Millett I.S., Jacob J., Zagrovic B., Dillon T.M., Cingel N., Dothager R.S., Seifert S., Thiyagarajan P.T., Sosnick T.R., Hasan M.Z., Pande V.S., Ruczinski I., Doniach S., and Plaxco K.W. Random-coil behavior and the dimensions of chemically unfolded proteins. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 12491-12496
22. Matsuo K., Sakurada Y., Yonehara R., Kataoka M., and Gekko K. Secondary-structure analysis of denatured proteins by vacuum-ultraviolet circular dichroism spectroscopy. Biophys. J. 92 (2007) 4088-4096
23. Privalov P.L., Mateo P.L., Khechinashvili N.N., Stepanov V.M., and Revina L.P. Comparative thermodynamic study of pepsinogen and pepsin structure. J. Mol. Biol. 152 (1981) 445-464
24. Lin X.L., Lin Y.Z., and Tang J. Relationships of human immunodeficiency virus protease with eukaryotic aspartic proteases. Methods Enzymol. 241 (1994) 195-224
25. Tanaka T., and Yada R.Y. N-terminal portion acts as an initiator of the inactivation of pepsin at neutral pH. Protein Eng. 14 (2001) 669-674
26. Maeda M., Takeuchi K., Kojima M., Tanokura M., Kimura K., Amemiya Y., Kihara H., and Takahashi K. Kinetic studies of unfolding process of aspergillopepsin II by pH-jump methods. Biochem. Biophys. Res. Commnun. 301 (2003) 745-750