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Volumn 10, Issue 2, 2009, Pages 390-399

Mutational analysis and allosteric effects in the HIV-1 capsid protein carboxyl-terminal dimerization domain

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC EFFECTS; CAPSID PROTEINS; CARBOXYL TERMINALS; CARBOXYL-TERMINAL DOMAINS; CONFORMATIONAL DYNAMICS; DIMERIZATION DOMAINS; DRIVING FORCES; HUMAN IMMUNODEFICIENCY VIRUS TYPE-1; HYDROPHOBIC CONTACTS; HYDROPHOBIC INTERACTIONS; LOCAL STRUCTURES; MUTATIONAL ANALYSIS; NATIVE CONFORMATIONS; SIDE CHAINS; STRUCTURAL CHANGES; STRUCTURAL STABILITIES; VIRAL CAPSIDS; VIRAL REPLICATIONS; WILD TYPES;

EID: 64149109477     PISSN: 15257797     EISSN: None     Source Type: Journal    
DOI: 10.1021/bm801151r     Document Type: Article
Times cited : (15)

References (41)
  • 2
    • 34848840882 scopus 로고    scopus 로고
    • How to assemble a capsid
    • Sundquist, W. I.; Hill, C. P. How to assemble a capsid. Cell 2007, 131 (1), 17-19.
    • (2007) Cell , vol.131 , Issue.1 , pp. 17-19
    • Sundquist, W.I.1    Hill, C.P.2
  • 4
    • 4043142786 scopus 로고    scopus 로고
    • Investigation of N-terminal domain charged residues on the assembly and stability of HIV-1CA
    • Douglas, C. C.; Thomas, D.; Lanman, J.; Prevelige, P. E. Investigation of N-terminal domain charged residues on the assembly and stability of HIV-1CA. Biochemistry 2004, 43 (32), 10435-10441.
    • (2004) Biochemistry , vol.43 , Issue.32 , pp. 10435-10441
    • Douglas, C.C.1    Thomas, D.2    Lanman, J.3    Prevelige, P.E.4
  • 6
    • 0029794123 scopus 로고    scopus 로고
    • Structure of the amino-terminal core domain of the HIV-1 capsid protein
    • Gitti, R. K.; Lee, B. M.; Walker, J.; Summers, M. F.; Yoo, S.; Sundquist, W. I. Structure of the amino-terminal core domain of the HIV-1 capsid protein. Science 1996, 273 (5272), 231-235.
    • (1996) Science , vol.273 , Issue.5272 , pp. 231-235
    • Gitti, R.K.1    Lee, B.M.2    Walker, J.3    Summers, M.F.4    Yoo, S.5    Sundquist, W.I.6
  • 7
    • 9644266693 scopus 로고    scopus 로고
    • Diversity and identity of mechanical properties of icosahedral viral capsids studied with elastic network normal mode analysis
    • Tama, F.; Brooks Iii, C. L. Diversity and identity of mechanical properties of icosahedral viral capsids studied with elastic network normal mode analysis. J. Mol. Biol. 2005, 345 (2), 299-314.
    • (2005) J. Mol. Biol , vol.345 , Issue.2 , pp. 299-314
    • Tama, F.1    Brooks Iii, C.L.2
  • 9
    • 0034699383 scopus 로고    scopus 로고
    • Image reconstructions of helical assemblies of the HIV-1 CA protein
    • Li, S.; Hill, C. P.; Sundquist, W. I.; Finch, J. T. Image reconstructions of helical assemblies of the HIV-1 CA protein. Nature 2000, 407 (6802), 409-413.
    • (2000) Nature , vol.407 , Issue.6802 , pp. 409-413
    • Li, S.1    Hill, C.P.2    Sundquist, W.I.3    Finch, J.T.4
  • 10
    • 26944455601 scopus 로고    scopus 로고
    • The HIV-1 capsid protein C-terminal domain in complex with a virus assembly inhibitor
    • Ternois, F.; Sticht, J.; Duquerroy, S.; Krausslich, H.-G.; Rey, F. A. The HIV-1 capsid protein C-terminal domain in complex with a virus assembly inhibitor. Nat. Struct. Mol. Biol. 2005, 12 (8), 678-682.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , Issue.8 , pp. 678-682
    • Ternois, F.1    Sticht, J.2    Duquerroy, S.3    Krausslich, H.-G.4    Rey, F.A.5
  • 11
    • 0028363103 scopus 로고
    • Specificity and sequence requirements for interactions between various retroviral Gag proteins
    • Franke, E. K.; Yuan, H. E.; Bossolt, K. L.; Goff, S. P.; Luban, J. Specificity and sequence requirements for interactions between various retroviral Gag proteins. J. Virol. 1994, 68 (8), 5300-5305.
    • (1994) J. Virol , vol.68 , Issue.8 , pp. 5300-5305
    • Franke, E.K.1    Yuan, H.E.2    Bossolt, K.L.3    Goff, S.P.4    Luban, J.5
  • 12
    • 0029961364 scopus 로고    scopus 로고
    • The role of Gag in human immunodeficiency virus type 1 virion morphogenesis and early steps of the viral life cycle
    • Reicin, A. S.; Ohagen, A.; Yin, L.; Hoglund, S.; Goff, S. P. The role of Gag in human immunodeficiency virus type 1 virion morphogenesis and early steps of the viral life cycle. J. Virol. 1996, 70 (12), 8645-8652.
    • (1996) J. Virol , vol.70 , Issue.12 , pp. 8645-8652
    • Reicin, A.S.1    Ohagen, A.2    Yin, L.3    Hoglund, S.4    Goff, S.P.5
  • 13
    • 0037388765 scopus 로고    scopus 로고
    • Structural organization of authentic, mature HIV-1 virions and cores
    • Briggs, J. A. G.; Wilk, T.; Welker, R.; Krausslich, H.-G.; Fuller, S. D. Structural organization of authentic, mature HIV-1 virions and cores. EMBO J. 2003, 22 (7), 1707-1715.
    • (2003) EMBO J , vol.22 , Issue.7 , pp. 1707-1715
    • Briggs, J.A.G.1    Wilk, T.2    Welker, R.3    Krausslich, H.-G.4    Fuller, S.D.5
  • 14
    • 34848866243 scopus 로고    scopus 로고
    • Structure of full-length HIV-1 CA: A model for the mature capsid lattice
    • Ganser-Pornillos, B. K.; Cheng, A.; Yeager, M. Structure of full-length HIV-1 CA: A model for the mature capsid lattice. Cell 2007, 131 (1), 70-79.
    • (2007) Cell , vol.131 , Issue.1 , pp. 70-79
    • Ganser-Pornillos, B.K.1    Cheng, A.2    Yeager, M.3
  • 15
    • 44949165530 scopus 로고    scopus 로고
    • Alcaraz, L. A.; '; Alamo, M. d.; Mateu, M. G.; Neira, J. L. Structural mobility of the monomeric C-terminal domain of the HIV-1 capsid protein. FEBS J. 2008, 275 (13), 3299-3311.
    • Alcaraz, L. A.; '; Alamo, M. d.; Mateu, M. G.; Neira, J. L. Structural mobility of the monomeric C-terminal domain of the HIV-1 capsid protein. FEBS J. 2008, 275 (13), 3299-3311.
  • 16
    • 0030448994 scopus 로고    scopus 로고
    • Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid
    • Gamble, T. R.; Vajdos, F. F.; Yoo, S.; Worthylake, D. K.; Houseweart, M.; Sundquist, W. I.; Hill, C. P. Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid. Cell 1996, 87 (7), 1285-1294.
    • (1996) Cell , vol.87 , Issue.7 , pp. 1285-1294
    • Gamble, T.R.1    Vajdos, F.F.2    Yoo, S.3    Worthylake, D.K.4    Houseweart, M.5    Sundquist, W.I.6    Hill, C.P.7
  • 17
    • 33644806492 scopus 로고    scopus 로고
    • The mechanism of HIV-1 core assembly: Insights from three-dimensional reconstructions of authentic virions
    • Briggs, J. A. G.; Grunewald, K.; Glass, B.; Forster, F.; Krausslich, H.-G.; Fuller, S. D. The mechanism of HIV-1 core assembly: insights from three-dimensional reconstructions of authentic virions. Structure 2006, 14 (1), 15-20.
    • (2006) Structure , vol.14 , Issue.1 , pp. 15-20
    • Briggs, J.A.G.1    Grunewald, K.2    Glass, B.3    Forster, F.4    Krausslich, H.-G.5    Fuller, S.D.6
  • 18
    • 47749116449 scopus 로고    scopus 로고
    • Atomistic simulations of the HIV-1 protease folding inhibition
    • Verkhivker, G.; Tiana, G.; Camilloni, C.; Provasi, D.; Broglia, R. A. Atomistic simulations of the HIV-1 protease folding inhibition. Biophys. J. 2008, 95 (2), 550-562.
    • (2008) Biophys. J , vol.95 , Issue.2 , pp. 550-562
    • Verkhivker, G.1    Tiana, G.2    Camilloni, C.3    Provasi, D.4    Broglia, R.A.5
  • 19
    • 0028342554 scopus 로고
    • Role of the major homology region of human immunodeficiency virus type 1 in virion morphogenesis
    • Mammano, F.; Ohagen, A.; Hoglund, S.; Gottlinger, H. G. Role of the major homology region of human immunodeficiency virus type 1 in virion morphogenesis. J. Virol. 1994, 68 (8), 4927-4936.
    • (1994) J. Virol , vol.68 , Issue.8 , pp. 4927-4936
    • Mammano, F.1    Ohagen, A.2    Hoglund, S.3    Gottlinger, H.G.4
  • 22
    • 0041784950 scopus 로고    scopus 로고
    • MacKerell, A. D.; Bashford, D.; Bellott, M.; Dunbrack, R. L.; Evanseck, J. D.; Field, M. J.; Fischer, S.; Gao, J.; Guo, H.; Ha, S.; Joseph-McCarthy, D.; Kuchnir, L.; Kuczera, K.; Lau, F. T. K.; Mattos, C.; Michnick, S.; Ngo, T.; Nguyen, D. T.; Prodhom, B.; Reiher, W. E.; Roux, B.; Schlenkrich, M.; Smith, J. C.; Stote, R.; Straub, J.; Watanabe, M.; Wiorkiewicz-Kuczera, J.; Yin, D.; Karplus, M. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B 1998, 102 (18), 3586-3616.
    • MacKerell, A. D.; Bashford, D.; Bellott, M.; Dunbrack, R. L.; Evanseck, J. D.; Field, M. J.; Fischer, S.; Gao, J.; Guo, H.; Ha, S.; Joseph-McCarthy, D.; Kuchnir, L.; Kuczera, K.; Lau, F. T. K.; Mattos, C.; Michnick, S.; Ngo, T.; Nguyen, D. T.; Prodhom, B.; Reiher, W. E.; Roux, B.; Schlenkrich, M.; Smith, J. C.; Stote, R.; Straub, J.; Watanabe, M.; Wiorkiewicz-Kuczera, J.; Yin, D.; Karplus, M. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B 1998, 102 (18), 3586-3616.
  • 23
    • 0242593434 scopus 로고    scopus 로고
    • Development and current status of the CHARMM force field for nucleic acids
    • MacKerell Jr, A. D.; Banavali, N.; Foloppe, N. Development and current status of the CHARMM force field for nucleic acids. Biopolymers 2000, 56 (4), 257-265.
    • (2000) Biopolymers , vol.56 , Issue.4 , pp. 257-265
    • MacKerell Jr, A.D.1    Banavali, N.2    Foloppe, N.3
  • 24
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • William, L. J.; Jayaraman, C.; Jeffry, D. M.; Roger, W. I.; Michael, L. K. Comparison of simple potential functions for simulating liquid water. J. Chem. Phys. 1983, 79 (2), 926-935.
    • (1983) J. Chem. Phys , vol.79 , Issue.2 , pp. 926-935
    • William, L.J.1    Jayaraman, C.2    Jeffry, D.M.3    Roger, W.I.4    Michael, L.K.5
  • 25
    • 0141956090 scopus 로고    scopus 로고
    • Generalized born model with a simple smoothing function
    • Im, W.; Lee, M. S.; Brooks, C. L., III. Generalized born model with a simple smoothing function. J. Comput. Chem. 2003, 24 (14), 1691-1702.
    • (2003) J. Comput. Chem , vol.24 , Issue.14 , pp. 1691-1702
    • Im, W.1    Lee, M.S.2    Brooks III, C.L.3
  • 26
    • 0242322528 scopus 로고    scopus 로고
    • An implicit membrane generalized born theory for the study of structure, stability, and interactions of membrane proteins
    • Im, W.; Feig, M.; Brooks, C. L. An implicit membrane generalized born theory for the study of structure, stability, and interactions of membrane proteins. Biophys. J. 2003, 85 (5), 2900-2918.
    • (2003) Biophys. J , vol.85 , Issue.5 , pp. 2900-2918
    • Im, W.1    Feig, M.2    Brooks, C.L.3
  • 27
    • 36148983867 scopus 로고    scopus 로고
    • Modeling the Alzheimer a{beta}17-42 fibril architecture: Tight intermolecular sheet-sheet association and intramolecular hydrated cavities
    • Zheng, J.; Jang, H.; Ma, B.; Tsai, C.-J.; Nussinov, R. Modeling the Alzheimer a{beta}17-42 fibril architecture: Tight intermolecular sheet-sheet association and intramolecular hydrated cavities. Biophys. J. 2007, 93 (9), 3046-3057.
    • (2007) Biophys. J , vol.93 , Issue.9 , pp. 3046-3057
    • Zheng, J.1    Jang, H.2    Ma, B.3    Tsai, C.-J.4    Nussinov, R.5
  • 28
    • 46749113483 scopus 로고    scopus 로고
    • Annular structures as intermediates in fibril formation of alzheimer A[beta]17-42
    • Zheng, J.; Jang, H.; Ma, B.; Nussinov, R. Annular structures as intermediates in fibril formation of alzheimer A[beta]17-42. J. Phys. Chem. B 2008, 112 (22), 6856-6865.
    • (2008) J. Phys. Chem. B , vol.112 , Issue.22 , pp. 6856-6865
    • Zheng, J.1    Jang, H.2    Ma, B.3    Nussinov, R.4
  • 29
    • 38949190032 scopus 로고    scopus 로고
    • Allosteric effects in the marginally stable von Hippel-Lindau tumor suppressor protein and allostery-based rescue mutant design
    • Liu, J.; Nussinov, R. Allosteric effects in the marginally stable von Hippel-Lindau tumor suppressor protein and allostery-based rescue mutant design. Proc. Natl. Acad. Sci. U.S.A. 2007, 105 (3), 901-906.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.105 , Issue.3 , pp. 901-906
    • Liu, J.1    Nussinov, R.2
  • 30
    • 39749090561 scopus 로고    scopus 로고
    • beta]2-microglobulin amyloid fragment organization and morphology and its comparison to A-[beta] suggests that amyloid aggregation pathways are sequence-specific
    • Zheng, J.; Jang, H.; Nussinov, R. [beta]2-microglobulin amyloid fragment organization and morphology and its comparison to A-[beta] suggests that amyloid aggregation pathways are sequence-specific. Biochemistry 2008, 47 (8), 2497-2509.
    • (2008) Biochemistry , vol.47 , Issue.8 , pp. 2497-2509
    • Zheng, J.1    Jang, H.2    Nussinov, R.3
  • 31
    • 33746765060 scopus 로고    scopus 로고
    • Structural stability and dynamics of an amyloid-forming peptide GNNQQNY from the yeast prion sup-35
    • Zheng, J.; Ma, B.; Tsai, C.-J.; Nussinov, R. Structural stability and dynamics of an amyloid-forming peptide GNNQQNY from the yeast prion sup-35. Biophys. J. 2006, 91 (3), 824-833.
    • (2006) Biophys. J , vol.91 , Issue.3 , pp. 824-833
    • Zheng, J.1    Ma, B.2    Tsai, C.-J.3    Nussinov, R.4
  • 32
    • 0036135139 scopus 로고    scopus 로고
    • A possible role for pi-stacking in the self-assembly of amyloid fibrils
    • Gazit, E. A possible role for pi-stacking in the self-assembly of amyloid fibrils. FASEB J. 2002, 16 (1), 77-83.
    • (2002) FASEB J , vol.16 , Issue.1 , pp. 77-83
    • Gazit, E.1
  • 33
    • 33846850446 scopus 로고    scopus 로고
    • Nanostructure design using protein building blocks enhanced by conformationally constrained synthetic residues
    • Zheng, J.; Zanuy, D.; Haspel, N.; Tsai, C. J.; Aleman, C.; Nussinov, R. Nanostructure design using protein building blocks enhanced by conformationally constrained synthetic residues. Biochemistry 2007, 46 (5), 1205-1218.
    • (2007) Biochemistry , vol.46 , Issue.5 , pp. 1205-1218
    • Zheng, J.1    Zanuy, D.2    Haspel, N.3    Tsai, C.J.4    Aleman, C.5    Nussinov, R.6
  • 34
    • 34447270230 scopus 로고    scopus 로고
    • Changing the charge distribution of {beta}-helical-based nano- structures can provide the conditions for charge transfer
    • Haspel, N.; Zanuy, D.; Zheng, J.; Aleman, C.; Wolfson, H.; Nussinov, R. Changing the charge distribution of {beta}-helical-based nano- structures can provide the conditions for charge transfer. Biophys. J. 2007, 93 (1), 245-253.
    • (2007) Biophys. J , vol.93 , Issue.1 , pp. 245-253
    • Haspel, N.1    Zanuy, D.2    Zheng, J.3    Aleman, C.4    Wolfson, H.5    Nussinov, R.6
  • 35
    • 42649088020 scopus 로고    scopus 로고
    • Molecular dynamics simulations of alzheimer's peptide A[beta]40 elongation and lateral association
    • Zheng, J.; Ma, B.; Chang, Y.; Nussinov, R. Molecular dynamics simulations of alzheimer's peptide A[beta]40 elongation and lateral association. Front. Biosci. 2008, 13 (1), 3919-3930.
    • (2008) Front. Biosci , vol.13 , Issue.1 , pp. 3919-3930
    • Zheng, J.1    Ma, B.2    Chang, Y.3    Nussinov, R.4
  • 36
    • 24344469405 scopus 로고    scopus 로고
    • An extensive thermodynamic characterization of the dimerization domain of the HIV-1 capsid protein
    • Lidon-Moya, M. C.; Barrera, F. N.; Bueno, M.; Perez-Jimenez, R.; Sancho, J.; Mateu, M. G.; Neira, J. L. An extensive thermodynamic characterization of the dimerization domain of the HIV-1 capsid protein. Protein Sci. 2005, 14 (9), 2387-2404.
    • (2005) Protein Sci , vol.14 , Issue.9 , pp. 2387-2404
    • Lidon-Moya, M.C.1    Barrera, F.N.2    Bueno, M.3    Perez-Jimenez, R.4    Sancho, J.5    Mateu, M.G.6    Neira, J.L.7
  • 37
    • 0041845304 scopus 로고    scopus 로고
    • Thermodynamic dissection of a low affinity protein-protein interface involved in human immu-nodeficiency virus assembly
    • del Alamo, M.; Neira, J. L.; Mateu, M. G. Thermodynamic dissection of a low affinity protein-protein interface involved in human immu-nodeficiency virus assembly. J. Biol. Chem. 2003, 278 (30), 27923-27929.
    • (2003) J. Biol. Chem , vol.278 , Issue.30 , pp. 27923-27929
    • del Alamo, M.1    Neira, J.L.2    Mateu, M.G.3
  • 38
    • 34548255898 scopus 로고    scopus 로고
    • Flexibility in HIV-1 assembly subunits: Solution structure of the monomeric C-terminal domain of the capsid protein
    • Alcaraz, L. A.; del Alamo, M.; Barrera, F. N.; Mateu, M. G.; Neira, J. L. Flexibility in HIV-1 assembly subunits: solution structure of the monomeric C-terminal domain of the capsid protein. Biophys. J. 2007, 93 (4), 1264-1276.
    • (2007) Biophys. J , vol.93 , Issue.4 , pp. 1264-1276
    • Alcaraz, L.A.1    del Alamo, M.2    Barrera, F.N.3    Mateu, M.G.4    Neira, J.L.5
  • 39
    • 52049093435 scopus 로고    scopus 로고
    • Damm, K. L.; Ung, P. M. U.; Quintero, J. J.; Gestwicki, J. E.; Carlson, H. A. A poke in the eye: Inhibiting HIV-1 protease through its flap- recognition pocket. Biopolymers 2008, 89 (8), 643-652.
    • Damm, K. L.; Ung, P. M. U.; Quintero, J. J.; Gestwicki, J. E.; Carlson, H. A. A poke in the eye: Inhibiting HIV-1 protease through its flap- recognition pocket. Biopolymers 2008, 89 (8), 643-652.
  • 40
    • 44949121782 scopus 로고    scopus 로고
    • Solution structure of HIV-1 protease flaps probed by comparison of molecular dynamics simulation ensembles and EPR experiments
    • Ding, F.; Layten, M.; Simmerling, C. Solution structure of HIV-1 protease flaps probed by comparison of molecular dynamics simulation ensembles and EPR experiments. J. Am. Chem. Soc. 2008, 130 (23), 7184-7185.
    • (2008) J. Am. Chem. Soc , vol.130 , Issue.23 , pp. 7184-7185
    • Ding, F.1    Layten, M.2    Simmerling, C.3
  • 41
    • 33644948688 scopus 로고    scopus 로고
    • HIV-1 protease flaps spontaneously close to the correct structure in simulations following manual placement of an inhibitor into the open state
    • Hornak, V.; Okur, A.; Rizzo, R. C.; Simmerling, C. HIV-1 protease flaps spontaneously close to the correct structure in simulations following manual placement of an inhibitor into the open state. J. Am. Chem. Soc. 2006, 128 (9), 2812-2813.
    • (2006) J. Am. Chem. Soc , vol.128 , Issue.9 , pp. 2812-2813
    • Hornak, V.1    Okur, A.2    Rizzo, R.C.3    Simmerling, C.4


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