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Volumn 108, Issue 52, 2011, Pages 20982-20987

Protein conformational dynamics in the mechanism of HIV-1 protease catalysis

Author keywords

Enzyme catalysis; Hiv protease; Protein dynamics; Protein nmr

Indexed keywords

HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE;

EID: 84855486395     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1111202108     Document Type: Article
Times cited : (80)

References (29)
  • 1
    • 0037624182 scopus 로고    scopus 로고
    • Twenty years of therapy for HIV-1 infection
    • DOI 10.1038/nm0703-867
    • Pomerantz RJ, Horn DL (2003) Twenty years of therapy for HIV-1 infection. Nat Med 9:867-873. (Pubitemid 36889928)
    • (2003) Nature Medicine , vol.9 , Issue.7 , pp. 867-873
    • Pomerantz, R.J.1    Horn, D.L.2
  • 2
    • 0028921302 scopus 로고
    • Flexibility and function in HIV-1 protease
    • Nicholson LK, et al. (1995) Flexibility and function in HIV-1 protease. Nat Struct Biol 2:274-280.
    • (1995) Nat Struct Biol , vol.2 , pp. 274-280
    • Nicholson, L.K.1
  • 3
    • 39749086224 scopus 로고    scopus 로고
    • A diverse view of protein dynamics from NMR studies of HIV-1 protease flaps
    • DOI 10.1002/prot.21632
    • Ishima R, Louis JM (2008) A diverse view of protein dynamics from NMR studies of HIV-1 protease flaps. Proteins 70:1408-1415. (Pubitemid 351304099)
    • (2008) Proteins: Structure, Function and Genetics , vol.70 , Issue.4 , pp. 1408-1415
    • Ishima, R.1    Louis, J.M.2
  • 4
    • 1842454635 scopus 로고    scopus 로고
    • HIV-1 protease molecular dynamics of a wild-type and of the V82F/I84V mutant: Possible contributions to drug resistance and a potential new target site for drugs
    • DOI 10.1110/ps.03468904
    • Perryman AL, Lin J-H, McCammon JA (2004) HIV-1 protease molecular dynamics of a wild-type and of the V82F/I84V mutant: Possible contributions to drug resistance and a potential new target site for drugs. Protein Sci 12:1108-1123. (Pubitemid 38429231)
    • (2004) Protein Science , vol.13 , Issue.4 , pp. 1108-1123
    • Perryman, A.L.1    Lin, J.-H.2    McCammon, J.A.3
  • 5
    • 33846635484 scopus 로고    scopus 로고
    • Targeting structural flexibility in HIV-1 protease inhibitor binding
    • DOI 10.1016/j.drudis.2006.12.011, PII S1359644606004934
    • Hornak V, Simmerling C (2007) Targeting structural flexibility in HIV-1 protease inhibitor binding. Drug Discov Today 12:132-138. (Pubitemid 46176670)
    • (2007) Drug Discovery Today , vol.12 , Issue.3-4 , pp. 132-138
    • Hornak, V.1    Simmerling, C.2
  • 6
    • 0036786493 scopus 로고    scopus 로고
    • Drug resistance in HIV-1 protease: Flexibility-assisted mechanism of compensatory mutations
    • Piana S, Carloni P, Rothlisberger U (2002) Drug resistance in HIV-1 protease: Flexibility-assisted mechanism of compensatory mutations. Protein Sci 11:2393-2402.
    • (2002) Protein Sci , vol.11 , pp. 2393-2402
    • Piana, S.1    Carloni, P.2    Rothlisberger, U.3
  • 7
    • 33744940504 scopus 로고    scopus 로고
    • Gated binding of ligands to HIV-1 protease: Brownian dynamics simulations in a coarse-grained model
    • DOI 10.1529/biophysj.105.074575
    • Chang C-E, Shen T, Trylska J, Tozzini V, McCammon JA (2006) Gated binding of ligands to HIV-1 protease: Brownian dynamics simulations in a coarse-grained model. Biophys J 90:3880-3885. (Pubitemid 43846106)
    • (2006) Biophysical Journal , vol.90 , Issue.11 , pp. 3880-3885
    • Chang, C.-E.1    Shen, T.2    Trylska, J.3    Tozzini, V.4    McCammon, J.A.5
  • 9
    • 48649102960 scopus 로고    scopus 로고
    • Crystal structure of chemically synthesized HIV-1 protease and a ketomethylene isostere inhibitor based on the p2/NC cleavage site
    • Torbeev VY, Mandal K, Terechko VA, Kent SBH (2008) Crystal structure of chemically synthesized HIV-1 protease and a ketomethylene isostere inhibitor based on the p2/NC cleavage site. Bioorg Med Chem Lett 18:4554-4557.
    • (2008) Bioorg Med Chem Lett , vol.18 , pp. 4554-4557
    • Torbeev, V.Y.1    Mandal, K.2    Terechko, V.A.3    Kent, S.B.H.4
  • 11
    • 77952055764 scopus 로고    scopus 로고
    • X-ray snapshot of HIV-1 protease in action: Observation of tetrahedral intermediate and short ionic hydrogen bond SIHB with catalytic aspartate
    • Das A, et al. (2010) X-ray snapshot of HIV-1 protease in action: Observation of tetrahedral intermediate and short ionic hydrogen bond SIHB with catalytic aspartate. J Am Chem Soc 132:6366-6373.
    • (2010) J Am Chem Soc , vol.132 , pp. 6366-6373
    • Das, A.1
  • 12
    • 0027944205 scopus 로고
    • Synthesis of proteins by native chemical ligation
    • Dawson PE, Muir TW, Clark-Lewis I, Kent SBH (1994) Synthesis of proteins by native chemical ligation. Science 266:776-779. (Pubitemid 24359280)
    • (1994) Science , vol.266 , Issue.5186 , pp. 776-779
    • Dawson, P.E.1    Muir, T.W.2    Clark-Lewis, I.3    Kent, S.B.H.4
  • 13
    • 33746299267 scopus 로고    scopus 로고
    • Kinetically controlled ligation for the convergent chemical synthesis of proteins
    • DOI 10.1002/anie.200600702
    • Bang D, Pentelute BL, Kent SBH (2006) Kinetically controlled ligation for the convergent chemical synthesis of proteins. Angew Chem Int Ed Engl 45:3985-3988. (Pubitemid 44105704)
    • (2006) Angewandte Chemie - International Edition , vol.45 , Issue.24 , pp. 3985-3988
    • Bang, D.1    Pentelute, B.L.2    Kent, S.B.H.3
  • 14
    • 34248230589 scopus 로고    scopus 로고
    • Convergent chemical synthesis and crystal structure of a 203 amino acid 'covalent dimer' HIV-1 protease enzyme molecule
    • DOI 10.1002/anie.200604087
    • Torbeev VY, Kent SBH (2007) Convergent chemical synthesis and crystal structure of a 203 amino acid 'covalent dimer' HIV-1 protease enzyme molecule. Angew Chem Int Ed Engl 46:1667-1670. (Pubitemid 46981347)
    • (2007) Angewandte Chemie - International Edition , vol.46 , Issue.10 , pp. 1667-1670
    • Torbeev, V.Yu.1    Kent, S.B.H.2
  • 17
    • 0034132251 scopus 로고    scopus 로고
    • Dead-time free measurement of dipole-dipole interactions between electron spins
    • Pannier M, Veit S, Godt A, Jeschke G, Spiess HW (2000) Dead-time free measurement of dipole-dipole interactions between electron spins. J Magn Reson 142:331-340.
    • (2000) J Magn Reson , vol.142 , pp. 331-340
    • Pannier, M.1    Veit, S.2    Godt, A.3    Jeschke, G.4    Spiess, H.W.5
  • 18
    • 61749086002 scopus 로고    scopus 로고
    • Dynamics of "flap" structures in three HIV-1 protease/inhibitor complexes probed by total chemical synthesis and pulse-EPR spectroscopy
    • Torbeev VY, et al. (2009) Dynamics of "flap" structures in three HIV-1 protease/inhibitor complexes probed by total chemical synthesis and pulse-EPR spectroscopy. J Am Chem Soc 131:884-885.
    • (2009) J Am Chem Soc , vol.131 , pp. 884-885
    • Torbeev, V.Y.1
  • 20
    • 33646911358 scopus 로고    scopus 로고
    • Fast time scale dynamics of protein backbones: NMR relaxation methods, applications, and functional consequences
    • DOI 10.1021/cr040421p
    • Jarymowycz VA, Stone MJ (2006) Fast time scale dynamics of protein backbones: NMR relaxation methods, applications, and functional consequences. Chem Rev 106:1624-1671. (Pubitemid 43792775)
    • (2006) Chemical Reviews , vol.106 , Issue.5 , pp. 1624-1671
    • Jarymowycz, V.A.1    Stone, M.J.2
  • 21
    • 0036147844 scopus 로고    scopus 로고
    • Rapid structural fluctuations of the free HIV protease flaps in solution: Relationship to crystal structures and comparison with predictions of dynamics calculations
    • DOI 10.1110/ps.33202
    • Freedberg DI, et al. (2002) Rapid structural fluctuations of the free HIV protease flaps in solution: Relationship to crystal structures and comparison with predictions of dynamic calculations. Protein Sci 11:221-232. (Pubitemid 34075785)
    • (2002) Protein Science , vol.11 , Issue.2 , pp. 221-232
    • Freedberg, D.I.1    Ishima, R.2    Jacob, J.3    Wang, Y.-X.4    Kustanovich, I.5    Louis, J.M.6    Torchia, D.A.7
  • 22
    • 0034919305 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for quantifying microsecond-to- millisecond motions in biological macromolecules
    • DOI 10.1016/S0076-6879(01)39315-1
    • Palmer AG, Kroenke CD, Loria JP (2001) Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules. Methods Enzymol 339:204-238. (Pubitemid 32666562)
    • (2001) Methods in Enzymology , vol.339 , pp. 204-238
    • Palmer III, A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 25
    • 0034711433 scopus 로고    scopus 로고
    • Protein backbone engineering through total chemical synthesis: New insight into the mechanism of HIV-1 protease catalysis
    • Baca M, Kent SBH (2000) Protein backbone engineering through total chemical synthesis: New insight into the mechanism of HIV-1 protease catalysis. Tetrahedron 56:9503-9513.
    • (2000) Tetrahedron , vol.56 , pp. 9503-9513
    • Baca, M.1    Kent, S.B.H.2
  • 26
    • 0023434194 scopus 로고
    • Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: Implications for a mechanism of action
    • Suguna K, Padlan EA, Smith CW, Carlson WD, Davies DR (1987) Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: Implications for a mechanism of action. Proc Natl Acad Sci USA 84:7009-7013.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7009-7013
    • Suguna, K.1    Padlan, E.A.2    Smith, C.W.3    Carlson, W.D.4    Davies, D.R.5
  • 27
    • 0025290527 scopus 로고
    • The structure and function of the aspartic proteinases
    • Davies DR (1990) The structure and function of the aspartic proteinases. Annu Rev Biophys Biophys Chem 19:189-215.
    • (1990) Annu Rev Biophys Biophys Chem , vol.19 , pp. 189-215
    • Davies, D.R.1
  • 28
    • 4043082181 scopus 로고    scopus 로고
    • Reaction mechanism of HIV-1 protease by hybrid Car-Parrinello/classical MD simulations
    • Piana S, Bucher D, Carloni P, Rothlisberger U (2004) Reaction mechanism of HIV-1 protease by hybrid Car-Parrinello/classical MD simulations. J Phys Chem B 108:11139-11149.
    • (2004) J Phys Chem B , vol.108 , pp. 11139-11149
    • Piana, S.1    Bucher, D.2    Carloni, P.3    Rothlisberger, U.4
  • 29
    • 0036882390 scopus 로고    scopus 로고
    • Structure and mechanism of the pepsin-like family of aspartic peptidases
    • Dunn BM (2002) Structure and mechanism of the pepsin-like family of aspartic peptidases. Chem Rev 102:4431-4458.
    • (2002) Chem Rev , vol.102 , pp. 4431-4458
    • Dunn, B.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.