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Volumn 19, Issue 11, 2010, Pages 2055-2072

Autocatalytic maturation, physical/chemical properties, and crystal structure of Group N HIV-1 protease: Relevance to drug resistance

Author keywords

Calorimetry; Crystal structure; Dimer dissociation; Enzyme kinetics; HIV AIDS; Polyprotein processing; Retroviral protease

Indexed keywords

AMINO ACID; DARUNAVIR; DIMER; MONOMER; PROTEINASE;

EID: 78349272713     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.486     Document Type: Article
Times cited : (23)

References (54)
  • 10
    • 17444392445 scopus 로고    scopus 로고
    • Autoprocessing of HIV-1 protease is tightly coupled to protein folding
    • Louis JM, Clore GM, Gronenborn AM (1999) Autoprocessing of HIV-1 protease is tightly coupled to protein folding. Nat Struct Biol 6:868-875.
    • (1999) Nat Struct Biol , vol.6 , pp. 868-875
    • Louis, J.M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 12
    • 73549092917 scopus 로고    scopus 로고
    • Fifteen years of HIV protease inhibitors: Raising the barrier to resistance
    • Wensing AM, van Maarseveen NM, Nijhuis M (2010) Fifteen years of HIV protease inhibitors: raising the barrier to resistance. Antiviral Res 85:59-74.
    • (2010) Antiviral Res , vol.85 , pp. 59-74
    • Wensing, A.M.1    Van Maarseveen, N.M.2    Nijhuis, M.3
  • 14
    • 40449087448 scopus 로고    scopus 로고
    • Inhibition of HIV-2 protease by HIV-1 protease inhibitors in clinical use
    • DOI 10.1111/j.1747-0285.2008.00647.x
    • Brower ET, Bacha UM, Kawasaki Y, Freire E (2008) Inhibition of HIV-2 protease by HIV-1 protease inhibitors in clinical use. Chem Biol Drug Des 71:298-305. (Pubitemid 351347797)
    • (2008) Chemical Biology and Drug Design , vol.71 , Issue.4 , pp. 298-305
    • Brower, E.T.1    Bacha, U.M.2    Kawasaki, Y.3    Freire, E.4
  • 15
    • 2942615093 scopus 로고    scopus 로고
    • The folding and dimerization of HIV-1 protease: Evidence for a stable monomer from simulations
    • DOI 10.1016/j.jmb.2004.04.028, PII S0022283604004425
    • Levy Y, Caflisch A, Onuchic JN, Wolynes PG (2004) The folding and dimerization of HIV-1 protease: evidence for a stable monomer from simulations. J Mol Biol 340:67-79. (Pubitemid 38739438)
    • (2004) Journal of Molecular Biology , vol.340 , Issue.1 , pp. 67-79
    • Levy, Y.1    Caflisch, A.2    Onuchic, J.N.3    Wolynes, P.G.4
  • 16
    • 0021912920 scopus 로고
    • Complete nucleotide sequence of the AIDS virus, HTLV-III
    • DOI 10.1038/313277a0
    • Ratner L, Haseltine W, Patarca R, Livak KJ, Starcich B, Josephs SF, Doran ER, Rafalski JA, Whitehorn EA, Baumeister K (1985) Complete nucleotide sequence of the AIDS virus, HTLV-III. Nature 313:277-284. (Pubitemid 15151982)
    • (1985) Nature , vol.313 , Issue.6000 , pp. 277-284
    • Ratner, L.1    Haseltine, W.2    Patarca, R.3
  • 18
    • 34447133502 scopus 로고    scopus 로고
    • Mutational and structural studies aimed at characterizing the monomer of HIV-1 protease and its precursor
    • DOI 10.1074/jbc.M701304200
    • Ishima R, Torchia DA, Louis JM (2007) Mutational and structural studies aimed at characterizing the monomer of HIV-1 protease and its precursor. J Biol Chem 282:17190-17199. (Pubitemid 47093202)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.23 , pp. 17190-17199
    • Ishima, R.1    Torchia, D.A.2    Louis, J.M.3
  • 19
    • 73149109097 scopus 로고    scopus 로고
    • Revealing the dimer dissociation and existence of a folded monomer of the mature HIV-2 protease
    • Louis JM, Ishima R, Aniana A, Sayer JM (2009) Revealing the dimer dissociation and existence of a folded monomer of the mature HIV-2 protease. Protein Sci 18:2442-2453.
    • (2009) Protein Sci , vol.18 , pp. 2442-2453
    • Louis, J.M.1    Ishima, R.2    Aniana, A.3    Sayer, J.M.4
  • 20
    • 0033525874 scopus 로고    scopus 로고
    • Stabilization from autoproteolysis and kinetic characterization of the human T-cell leukemia virus type 1 proteinase
    • DOI 10.1074/jbc.274.10.6660
    • Louis JM, Oroszlan S, Tozser J (1999) Stabilization from autoproteolysis and kinetic characterization of the human T-cell leukemia virus type 1 proteinase. J Biol Chem 274:6660-6666. (Pubitemid 29111086)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.10 , pp. 6660-6666
    • Louis, J.M.1    Oroszlan, S.2    Tozser, J.3
  • 22
    • 0242353303 scopus 로고    scopus 로고
    • Solution Structure of the Mature HIV-1 Protease Monomer: Insight into the tertiary fold and stability of a precursor
    • DOI 10.1074/jbc.M307549200
    • Ishima R, Torchia DA, Lynch SM, Gronenborn AM, Louis JM (2003) Solution structure of the mature HIV-1 protease monomer: insight into the tertiary fold and stability of a precursor. J Biol Chem 278:43311-43319. (Pubitemid 37345952)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.44 , pp. 43311-43319
    • Ishima, R.1    Torchia, D.A.2    Lynch, S.M.3    Gronenborn, A.M.4    Louis, J.M.5
  • 23
    • 0029913459 scopus 로고    scopus 로고
    • Conformational stability and catalytic activity of HIV-1 protease are both enhanced at high salt concentration
    • DOI 10.1074/jbc.271.10.5458
    • Szeltner Z, Polgar L (1996) Conformational stability and catalytic activity of HIV-1 protease are both enhanced at high salt concentration. J Biol Chem 271:5458-5463. (Pubitemid 26083878)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.10 , pp. 5458-5463
    • Szeltner, Z.1    Polgar, L.2
  • 24
    • 45149083375 scopus 로고    scopus 로고
    • Effect of the active-site D25N mutation on the structure, stability and ligand binding of the mature HIV-1 protease
    • Sayer JM, Liu F, Ishima R, Weber IT, Louis JM (2008) Effect of the active-site D25N mutation on the structure, stability and ligand binding of the mature HIV-1 protease. J Biol Chem 283:13459-13470.
    • (2008) J Biol Chem , vol.283 , pp. 13459-13470
    • Sayer, J.M.1    Liu, F.2    Ishima, R.3    Weber, I.T.4    Louis, J.M.5
  • 25
    • 66149111430 scopus 로고    scopus 로고
    • Interactions of different inhibitors with active-site aspartyl residues of HIV-1 protease and possible relevance to pepsin
    • Sayer JM, Louis JM (2008) Interactions of different inhibitors with active-site aspartyl residues of HIV-1 protease and possible relevance to pepsin. Proteins 75:556-568.
    • (2008) Proteins , vol.75 , pp. 556-568
    • Sayer, J.M.1    Louis, J.M.2
  • 27
    • 34250641961 scopus 로고    scopus 로고
    • Isothermal titration calorimetry to determine association constants for high-affinity ligands
    • Velazquez-Campoy A, Freire E (2006) Isothermal titration calorimetry to determine association constants for high-affinity ligands. Nat Protoc 1:186-191.
    • (2006) Nat Protoc , vol.1 , pp. 186-191
    • Velazquez-Campoy, A.1    Freire, E.2
  • 28
    • 6344231715 scopus 로고    scopus 로고
    • Structural and thermodynamic basis for the binding of TMC114, a next-generation human immunodeficiency virus type 1 protease inhibitor
    • DOI 10.1128/JVI.78.21.12012-12021.2004
    • King NM, Prabu-Jeyabalan M, Nalivaika EA, Wigerinck P, de Bethune MP, Schiffer CA (2004) Structural and thermodynamic basis for the binding of TMC114, a next-generation human immunodeficiency virus type 1 protease inhibitor. J Virol 78:12012-12021. (Pubitemid 39390785)
    • (2004) Journal of Virology , vol.78 , Issue.21 , pp. 12012-12021
    • King, N.M.1    Prabu-Jeyabalan, M.2    Nalivaika, E.A.3    Wigerinck, P.4    De Bethune, M.-P.5    Schiffer, C.A.6
  • 29
    • 0141571239 scopus 로고    scopus 로고
    • Covariation of amino acid positions in HIV-1 protease
    • DOI 10.1016/S0042-6822(03)00484-7
    • Hoffman NG, Schiffer CA, Swanstrom R (2003) Covariation of amino acid positions in HIV-1 protease. Virology 314:536-548. (Pubitemid 37206360)
    • (2003) Virology , vol.314 , Issue.2 , pp. 536-548
    • Hoffman, N.G.1    Schiffer, C.A.2    Swanstrom, R.3
  • 30
    • 0036298514 scopus 로고    scopus 로고
    • Relation between sequence and structure of HIV-1 protease inhibitor complexes: A model system for the analysis of protein Flexibility
    • DOI 10.1006/jmbi.2001.5173
    • Zoete V, Michielin O, Karplus M (2002) Relation between sequence and structure of HIV-1 protease inhibitor complexes: a model system for the analysis of protein flexibility. J Mol Biol 315:21-52. (Pubitemid 34722109)
    • (2002) Journal of Molecular Biology , vol.315 , Issue.1 , pp. 21-52
    • Zoete, V.1    Michielin, O.2    Karplus, M.3
  • 31
    • 34248586556 scopus 로고    scopus 로고
    • Structural Characterization of B and non-B Subtypes of HIV-Protease: Insights into the Natural Susceptibility to Drug Resistance Development
    • DOI 10.1016/j.jmb.2007.03.049, PII S0022283607004032
    • Sanches M, Krauchenco S, Martins NH, Gustchina A, Wlodawer A, Polikarpov I (2007) Structural characterization of B and non-B subtypes of HIV-protease: insights into the natural susceptibility to drug resistance development. J Mol Biol 369:1029-1040. (Pubitemid 46754060)
    • (2007) Journal of Molecular Biology , vol.369 , Issue.4 , pp. 1029-1040
    • Sanches, M.1    Krauchenco, S.2    Martins, N.H.3    Gustchina, A.4    Wlodawer, A.5    Polikarpov, I.6
  • 32
    • 38849209120 scopus 로고    scopus 로고
    • The contribution of naturally occurring polymorphisms in altering the biochemical and structural characteristics of HIV-1 subtype C protease
    • DOI 10.1021/bi7018332
    • Coman RM, Robbins AH, Fernandez MA, Gilliland CT, Sochet AA, Goodenow MM, McKenna R, Dunn BM (2008) The contribution of naturally occurring polymorphisms in altering the biochemical and structural characteristics of HIV-1 subtype C protease. Biochemistry 47:731-743. (Pubitemid 351195444)
    • (2008) Biochemistry , vol.47 , Issue.2 , pp. 731-743
    • Coman, R.M.1    Robbins, A.H.2    Fernandez, M.A.3    Gilliland, C.T.4    Sochet, A.A.5    Goodenow, M.M.6    McKenna, R.7    Dunn, B.M.8
  • 34
    • 0038298453 scopus 로고    scopus 로고
    • Polymorphism in HIV-1 non-subtype b protease and reverse transcriptase and its potential impact on drug susceptibility and drug resistance evolution
    • Kantor R, Katzenstein D (2003) Polymorphism in HIV-1 non-subtype B protease and reverse transcriptase and its potential impact on drug susceptibility and drug resistance evolution. AIDS Rev 5:25-35. (Pubitemid 36873892)
    • (2003) AIDS Reviews , vol.5 , Issue.1 , pp. 25-35
    • Kantor, R.1    Katzenstein, D.2
  • 35
    • 34250177944 scopus 로고    scopus 로고
    • Computational Characterization of Structural Role of the Non-active Site Mutation M36I of Human Immunodeficiency Virus Type 1 Protease
    • DOI 10.1016/j.jmb.2007.04.081, PII S0022283607005840
    • Ode H, Matsuyama S, Hata M, Neya S, Kakizawa J, Sugiura W, Hoshino T (2007) Computational characterization of structural role of the non-active site mutation M36I of human immunodeficiency virus type 1 protease. J Mol Biol 370:598-607. (Pubitemid 46901071)
    • (2007) Journal of Molecular Biology , vol.370 , Issue.3 , pp. 598-607
    • Ode, H.1    Matsuyama, S.2    Hata, M.3    Neya, S.4    Kakizawa, J.5    Sugiura, W.6    Hoshino, T.7
  • 37
    • 0033778181 scopus 로고    scopus 로고
    • Crystal structure of an in vivo HIV-1 protease mutant in complex with saquinavir: Insights into the mechanisms of drug resistance
    • Hong L, Zhang XC, Hartsuck JA, Tang J (2000) Crystal structure of an in vivo HIV-1 protease mutant in complex with saquinavir: insights into the mechanisms of drug resistance. Protein Sci 9:1898-1904.
    • (2000) Protein Sci , vol.9 , pp. 1898-1904
    • Hong, L.1    Zhang, X.C.2    Hartsuck, J.A.3    Tang, J.4
  • 39
    • 78349268413 scopus 로고    scopus 로고
    • HIV-1 protease: Structural perspectives on drug resistance
    • Agniswamy J, Weber IT (2009) HIV-1 protease: structural perspectives on drug resistance. Viruses 1:1110-1136.
    • (2009) Viruses , vol.1 , pp. 1110-1136
    • Agniswamy, J.1    Weber, I.T.2
  • 40
    • 11144354478 scopus 로고    scopus 로고
    • High resolution crystal structures of HIV-1 protease with a potent non-peptide inhibitor (UIC-94017) active against multi-drug-resistant clinical strains
    • DOI 10.1016/j.jmb.2004.02.052, PII S0022283604002323
    • Tie Y, Boross PI, Wang YF, Gaddis L, Hussain AK, Leshchenko S, Ghosh AK, Louis JM, Harrison RW, Weber IT (2004) High resolution crystal structures of HIV-1 protease with a potent non-peptide inhibitor (UIC-94017) active against multi-drug-resistant clinical strains. J Mol Biol 338:341-352. (Pubitemid 38447090)
    • (2004) Journal of Molecular Biology , vol.338 , Issue.2 , pp. 341-352
    • Tie, Y.1    Boross, P.I.2    Wang, Y.-F.3    Gaddis, L.4    Hussain, A.K.5    Leshchenko, S.6    Ghosh, A.K.7    Louis, J.M.8    Harrison, R.W.9    Weber, I.T.10
  • 42
    • 46649092697 scopus 로고    scopus 로고
    • Effect of flap mutations on structure of HIV-1 protease and inhibition by saquinavir and darunavir
    • Liu F, Kovalevsky AY, Tie Y, Ghosh AK, Harrison RW, Weber IT (2008) Effect of flap mutations on structure of HIV-1 protease and inhibition by saquinavir and darunavir. J Mol Biol 381:102-115.
    • (2008) J Mol Biol , vol.381 , pp. 102-115
    • Liu, F.1    Kovalevsky, A.Y.2    Tie, Y.3    Ghosh, A.K.4    Harrison, R.W.5    Weber, I.T.6
  • 43
    • 53349152834 scopus 로고    scopus 로고
    • Visualizing transient events in amino-terminal autoprocessing of HIV-1 protease
    • Tang C, Louis JM, Aniana A, Suh JY, Clore GM (2008) Visualizing transient events in amino-terminal autoprocessing of HIV-1 protease. Nature 455:693-696.
    • (2008) Nature , vol.455 , pp. 693-696
    • Tang, C.1    Louis, J.M.2    Aniana, A.3    Suh, J.Y.4    Clore, G.M.5
  • 44
    • 0032562202 scopus 로고    scopus 로고
    • Hydrophilic peptides derived from the transframe region of Gag-Pol inhibit the HIV-1 protease
    • DOI 10.1021/bi972059x
    • Louis JM, Dyda F, Nashed NT, Kimmel AR, Davies DR (1998) Hydrophilic peptides derived from the transframe region of Gag-Pol inhibit the HIV-1 protease. Biochemistry 37:2105-2110. (Pubitemid 28119284)
    • (1998) Biochemistry , vol.37 , Issue.8 , pp. 2105-2110
    • Louis, J.M.1    Dyda, F.2    Nashed, N.T.3    Kimmel, A.R.4    Davies, D.R.5
  • 46
    • 0029417217 scopus 로고
    • In vivo processing of Pr160gag-pol from human immunodeficiency virus type 1 (HIV) in acutely infected, cultured human T-lymphocytes
    • Lindhofer H, von der Helm K, Nitschko H (1995) In vivo processing of Pr160gag-pol from human immunodeficiency virus type 1 (HIV) in acutely infected, cultured human T-lymphocytes. Virology 214:624-627.
    • (1995) Virology , vol.214 , pp. 624-627
    • Lindhofer, H.1    Von Der Helm, K.2    Nitschko, H.3
  • 47
    • 0036428535 scopus 로고    scopus 로고
    • Modulation of the oligomeric structures of HIV-1 retroviral enzymes by synthetic peptides and small molecules
    • DOI 10.1046/j.1432-1033.2002.03216.x
    • Sluis-Cremer N, Tachedjian G (2002) Modulation of the oligomeric structures of HIV-1 retroviral enzymes by synthetic peptides and small molecules. Eur J Biochem 269:5103-5111. (Pubitemid 35340819)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.21 , pp. 5103-5111
    • Sluis-Cremer, N.1    Tachedjian, G.2
  • 49
    • 0032561137 scopus 로고    scopus 로고
    • The structural stability of the HIV-1 protease
    • Todd MJ, Semo N, Freire E (1998) The structural stability of the HIV-1 protease. J Mol Biol 283:475-488.
    • (1998) J Mol Biol , vol.283 , pp. 475-488
    • Todd, M.J.1    Semo, N.2    Freire, E.3
  • 50
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data in oscillation mode
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data in oscillation mode. Methods Enzymol 276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 54


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