메뉴 건너뛰기




Volumn 106, Issue 5, 2014, Pages 1142-1151

A flexible docking scheme efficiently captures the energetics of glycan-cyanovirin binding

Author keywords

[No Author keywords available]

Indexed keywords

ANTI HUMAN IMMUNODEFICIENCY VIRUS AGENT; BACTERIAL PROTEIN; CARRIER PROTEIN; CYANOVIRIN N; POLYSACCHARIDE;

EID: 84901743765     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2014.01.040     Document Type: Article
Times cited : (11)

References (58)
  • 1
    • 0035112229 scopus 로고    scopus 로고
    • Cyanovirin-N, a potent human immunodeficiency virus-inactivating protein, blocks both CD4-dependent and CD4-independent binding of soluble gp120 (sgp120) to target cells, inhibits sCD4-induced binding of sgp120 to cell-associated CXCR4, and dissociates bound sgp120 from target cells
    • T. Mori, and M.R. Boyd Cyanovirin-N, a potent human immunodeficiency virus-inactivating protein, blocks both CD4-dependent and CD4-independent binding of soluble gp120 (sgp120) to target cells, inhibits sCD4-induced binding of sgp120 to cell-associated CXCR4, and dissociates bound sgp120 from target cells Antimicrob. Agents Chemother. 45 2001 664 672
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 664-672
    • Mori, T.1    Boyd, M.R.2
  • 2
    • 0032921247 scopus 로고    scopus 로고
    • Cyanovirin-N binds to gp120 to interfere with CD4-dependent human immunodeficiency virus type 1 virion binding, fusion, and infectivity but does not affect the CD4 binding site on gp120 or soluble CD4-induced conformational changes in gp120
    • M.T. Esser, and T. Mori J.D. Lifson Cyanovirin-N binds to gp120 to interfere with CD4-dependent human immunodeficiency virus type 1 virion binding, fusion, and infectivity but does not affect the CD4 binding site on gp120 or soluble CD4-induced conformational changes in gp120 J. Virol. 73 1999 4360 4371
    • (1999) J. Virol. , vol.73 , pp. 4360-4371
    • Esser, M.T.1    Mori, T.2    Lifson, J.D.3
  • 3
    • 0037300816 scopus 로고    scopus 로고
    • Cyanovirin-N: A sugar-binding antiviral protein with a new twist
    • I. Botos, and A. Wlodawer Cyanovirin-N: a sugar-binding antiviral protein with a new twist Cell. Mol. Life Sci. 60 2003 277 287
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 277-287
    • Botos, I.1    Wlodawer, A.2
  • 4
    • 0242586063 scopus 로고    scopus 로고
    • Cyanovirin-N binds to the viral surface glycoprotein, GP1,2 and inhibits infectivity of Ebola virus
    • L.G. Barrientos, and B.R. O'Keefe M.R. Boyd Cyanovirin-N binds to the viral surface glycoprotein, GP1,2 and inhibits infectivity of Ebola virus Antiviral Res. 58 2003 47 56
    • (2003) Antiviral Res. , vol.58 , pp. 47-56
    • Barrientos, L.G.1    O'Keefe, B.R.2    Boyd, M.R.3
  • 5
    • 0035028207 scopus 로고    scopus 로고
    • Cyanovirin-N defines a new class of antiviral agent targeting N-linked, high-mannose glycans in an oligosaccharide-specific manner
    • A.J. Bolmstedt, and B.R. O'Keefe M.R. Boyd Cyanovirin-N defines a new class of antiviral agent targeting N-linked, high-mannose glycans in an oligosaccharide-specific manner Mol. Pharmacol. 59 2001 949 954
    • (2001) Mol. Pharmacol. , vol.59 , pp. 949-954
    • Bolmstedt, A.J.1    O'Keefe, B.R.2    Boyd, M.R.3
  • 6
    • 34447523910 scopus 로고    scopus 로고
    • Targeting the glycans of glycoproteins: A novel paradigm for antiviral therapy
    • J. Balzarini Targeting the glycans of glycoproteins: a novel paradigm for antiviral therapy Nat. Rev. Microbiol. 5 2007 583 597
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 583-597
    • Balzarini, J.1
  • 7
    • 34247636624 scopus 로고    scopus 로고
    • Exploiting the defensive sugars of HIV-1 for drug and vaccine design
    • C.N. Scanlan, and J. Offer R.A. Dwek Exploiting the defensive sugars of HIV-1 for drug and vaccine design Nature 446 2007 1038 1045
    • (2007) Nature , vol.446 , pp. 1038-1045
    • Scanlan, C.N.1    Offer, J.2    Dwek, R.A.3
  • 8
    • 43049111403 scopus 로고    scopus 로고
    • Conformational gating of dimannose binding to the antiviral protein cyanovirin revealed from the crystal structure at 1.35 A resolution
    • R. Fromme, and Z. Katiliene G. Ghirlanda Conformational gating of dimannose binding to the antiviral protein cyanovirin revealed from the crystal structure at 1.35 A resolution Protein Sci. 17 2008 939 944
    • (2008) Protein Sci. , vol.17 , pp. 939-944
    • Fromme, R.1    Katiliene, Z.2    Ghirlanda, G.3
  • 9
    • 34547916495 scopus 로고    scopus 로고
    • A monovalent mutant of cyanovirin-N provides insight into the role of multiple interactions with gp120 for antiviral activity
    • R. Fromme, and Z. Katiliene G. Ghirlanda A monovalent mutant of cyanovirin-N provides insight into the role of multiple interactions with gp120 for antiviral activity Biochemistry 46 2007 9199 9207
    • (2007) Biochemistry , vol.46 , pp. 9199-9207
    • Fromme, R.1    Katiliene, Z.2    Ghirlanda, G.3
  • 10
    • 67549112686 scopus 로고    scopus 로고
    • Multivalent interactions with gp120 are required for the anti-HIV activity of Cyanovirin
    • Y. Liu, and J.R. Carroll G. Ghirlanda Multivalent interactions with gp120 are required for the anti-HIV activity of Cyanovirin Biopolymers 92 2009 194 200
    • (2009) Biopolymers , vol.92 , pp. 194-200
    • Liu, Y.1    Carroll, J.R.2    Ghirlanda, G.3
  • 11
    • 77951219869 scopus 로고    scopus 로고
    • Anti-HIV activity of defective cyanovirin-N mutants is restored by dimerization
    • E. Matei, and A. Zheng A.M. Gronenborn Anti-HIV activity of defective cyanovirin-N mutants is restored by dimerization J. Biol. Chem. 285 2010 13057 13065
    • (2010) J. Biol. Chem. , vol.285 , pp. 13057-13065
    • Matei, E.1    Zheng, A.2    Gronenborn, A.M.3
  • 12
    • 80052169440 scopus 로고    scopus 로고
    • Designed oligomers of cyanovirin-N show enhanced HIV neutralization
    • J.R. Keeffe, and P.N.P. Gnanapragasam S.L. Mayo Designed oligomers of cyanovirin-N show enhanced HIV neutralization Proc. Natl. Acad. Sci. USA 108 2011 14079 14084
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 14079-14084
    • Keeffe, J.R.1    Gnanapragasam, P.N.P.2    Mayo, S.L.3
  • 13
    • 82955169560 scopus 로고    scopus 로고
    • Rational and computational design of stabilized variants of cyanovirin-N that retain affinity and specificity for glycan ligands
    • V. Patsalo, D.P. Raleigh, and D.F. Green Rational and computational design of stabilized variants of cyanovirin-N that retain affinity and specificity for glycan ligands Biochemistry 50 2011 10698 10712
    • (2011) Biochemistry , vol.50 , pp. 10698-10712
    • Patsalo, V.1    Raleigh, D.P.2    Green, D.F.3
  • 14
    • 41449109826 scopus 로고    scopus 로고
    • The evolutionarily conserved family of cyanovirin-N homologs: Structures and carbohydrate specificity
    • L.M.I. Koharudin, and A.R. Viscomi A.M. Gronenborn The evolutionarily conserved family of cyanovirin-N homologs: structures and carbohydrate specificity Structure 16 2008 570 584
    • (2008) Structure , vol.16 , pp. 570-584
    • Koharudin, L.M.I.1    Viscomi, A.R.2    Gronenborn, A.M.3
  • 15
    • 0034799906 scopus 로고    scopus 로고
    • The potent anti-HIV protein cyanovirin-N contains two novel carbohydrate binding sites that selectively bind to Man(8) D1D3 and Man(9) with nanomolar affinity: Implications for binding to the HIV envelope protein gp120
    • C.A. Bewley, and S. Otero-Quintero The potent anti-HIV protein cyanovirin-N contains two novel carbohydrate binding sites that selectively bind to Man(8) D1D3 and Man(9) with nanomolar affinity: implications for binding to the HIV envelope protein gp120 J. Am. Chem. Soc. 123 2001 3892 3902
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 3892-3902
    • Bewley, C.A.1    Otero-Quintero, S.2
  • 16
    • 48149091784 scopus 로고    scopus 로고
    • Solution and crystal structures of a sugar binding site mutant of cyanovirin-N: No evidence of domain swapping
    • E. Matei, W. Furey, and A.M. Gronenborn Solution and crystal structures of a sugar binding site mutant of cyanovirin-N: no evidence of domain swapping Structure 16 2008 1183 1194
    • (2008) Structure , vol.16 , pp. 1183-1194
    • Matei, E.1    Furey, W.2    Gronenborn, A.M.3
  • 17
    • 55549091754 scopus 로고    scopus 로고
    • Computational models explain the oligosaccharide specificity of cyanovirin-N
    • Y.K. Fujimoto, and R.N. Terbush D.F. Green Computational models explain the oligosaccharide specificity of cyanovirin-N Protein Sci. 17 2008 2008 2014
    • (2008) Protein Sci. , vol.17 , pp. 2008-2014
    • Fujimoto, Y.K.1    Terbush, R.N.2    Green, D.F.3
  • 18
    • 0034791996 scopus 로고    scopus 로고
    • Solution structure of a cyanovirin-N:Man α1-2Man α complex: Structural basis for high-affinity carbohydrate-mediated binding to gp120
    • C.A. Bewley Solution structure of a cyanovirin-N:Man α1-2Man α complex: structural basis for high-affinity carbohydrate-mediated binding to gp120 Structure 9 2001 931 940
    • (2001) Structure , vol.9 , pp. 931-940
    • Bewley, C.A.1
  • 19
    • 0037072880 scopus 로고    scopus 로고
    • Structures of the complexes of a potent anti-HIV protein cyanovirin-N and high mannose oligosaccharides
    • I. Botos, and B.R. O'Keefe A. Wlodawer Structures of the complexes of a potent anti-HIV protein cyanovirin-N and high mannose oligosaccharides J. Biol. Chem. 277 2002 34336 34342
    • (2002) J. Biol. Chem. , vol.277 , pp. 34336-34342
    • Botos, I.1    O'Keefe, B.R.2    Wlodawer, A.3
  • 20
    • 14844351573 scopus 로고    scopus 로고
    • Computational study of the dynamics of mannose disaccharides free in solution and bound to the potent anti-HIV virucidal protein cyanovirin
    • C.J. Margulis Computational study of the dynamics of mannose disaccharides free in solution and bound to the potent anti-HIV virucidal protein cyanovirin J. Phys. Chem. B 109 2005 3639 3647
    • (2005) J. Phys. Chem. B , vol.109 , pp. 3639-3647
    • Margulis, C.J.1
  • 21
    • 72249105167 scopus 로고    scopus 로고
    • Solution and crystal molecular dynamics simulation study of m4-cyanovirin-N mutants complexed with di-mannose
    • I.I. Vorontsov, and O. Miyashita Solution and crystal molecular dynamics simulation study of m4-cyanovirin-N mutants complexed with di-mannose Biophys. J. 97 2009 2532 2540
    • (2009) Biophys. J. , vol.97 , pp. 2532-2540
    • Vorontsov, I.I.1    Miyashita, O.2
  • 22
    • 0036389940 scopus 로고    scopus 로고
    • Site-specific discrimination by cyanovirin-N for α-linked trisaccharides comprising the three arms of Man(8) and Man(9)
    • C.A. Bewley, S. Kiyonaka, and I. Hamachi Site-specific discrimination by cyanovirin-N for α-linked trisaccharides comprising the three arms of Man(8) and Man(9) J. Mol. Biol. 322 2002 881 889
    • (2002) J. Mol. Biol. , vol.322 , pp. 881-889
    • Bewley, C.A.1    Kiyonaka, S.2    Hamachi, I.3
  • 23
    • 0036773694 scopus 로고    scopus 로고
    • Multisite and multivalent binding between cyanovirin-N and branched oligomannosides: Calorimetric and NMR characterization
    • S.R. Shenoy, and L.G. Barrientos M.R. Boyd Multisite and multivalent binding between cyanovirin-N and branched oligomannosides: calorimetric and NMR characterization Chem. Biol. 9 2002 1109 1118
    • (2002) Chem. Biol. , vol.9 , pp. 1109-1118
    • Shenoy, S.R.1    Barrientos, L.G.2    Boyd, M.R.3
  • 24
    • 8344235090 scopus 로고    scopus 로고
    • Atomic mapping of the interactions between the antiviral agent cyanovirin-N and oligomannosides by saturation-transfer difference NMR
    • C. Sandström, and O. Berteau A.M. Gronenborn Atomic mapping of the interactions between the antiviral agent cyanovirin-N and oligomannosides by saturation-transfer difference NMR Biochemistry 43 2004 13926 13931
    • (2004) Biochemistry , vol.43 , pp. 13926-13931
    • Sandström, C.1    Berteau, O.2    Gronenborn, A.M.3
  • 25
    • 84884648529 scopus 로고    scopus 로고
    • The antiviral lectin cyanovirin-N: Probing multivalency and glycan recognition through experimental and computational approaches
    • B.W. Woodrum, and J.D. Maxwell G. Ghirlanda The antiviral lectin cyanovirin-N: probing multivalency and glycan recognition through experimental and computational approaches Biochem. Soc. Trans. 41 2013 1170 1176
    • (2013) Biochem. Soc. Trans. , vol.41 , pp. 1170-1176
    • Woodrum, B.W.1    Maxwell, J.D.2    Ghirlanda, G.3
  • 26
    • 77955680967 scopus 로고    scopus 로고
    • Manipulation of conformational change in proteins by single-residue perturbations
    • C. Atilgan, and Z.N. Gerek A.R. Atilgan Manipulation of conformational change in proteins by single-residue perturbations Biophys. J. 99 2010 933 943
    • (2010) Biophys. J. , vol.99 , pp. 933-943
    • Atilgan, C.1    Gerek, Z.N.2    Atilgan, A.R.3
  • 27
    • 77951588413 scopus 로고    scopus 로고
    • A flexible docking scheme to explore the binding selectivity of PDZ domains
    • Z.N. Gerek, and S.B. Ozkan A flexible docking scheme to explore the binding selectivity of PDZ domains Protein Sci. 19 2010 914 928
    • (2010) Protein Sci. , vol.19 , pp. 914-928
    • Gerek, Z.N.1    Ozkan, S.B.2
  • 28
    • 80055066238 scopus 로고    scopus 로고
    • Change in allosteric network affects binding affinities of PDZ domains: Analysis through perturbation response scanning
    • Z.N. Gerek, and S.B. Ozkan Change in allosteric network affects binding affinities of PDZ domains: analysis through perturbation response scanning PLOS Comput. Biol. 7 2011 e1002154
    • (2011) PLOS Comput. Biol. , vol.7 , pp. 1002154
    • Gerek, Z.N.1    Ozkan, S.B.2
  • 29
    • 84859444323 scopus 로고    scopus 로고
    • The binding affinities of proteins interacting with the PDZ domain of PICK1
    • A. Bolia, and Z.N. Gerek K.K. Dev The binding affinities of proteins interacting with the PDZ domain of PICK1 Proteins 80 2012 1393 1408
    • (2012) Proteins , vol.80 , pp. 1393-1408
    • Bolia, A.1    Gerek, Z.N.2    Dev, K.K.3
  • 30
    • 70449492577 scopus 로고    scopus 로고
    • Computational study of the conformational structures of saccharides in solution based on J couplings and the "fast sugar structure prediction software"
    • J. Xia, and C.J. Margulis Computational study of the conformational structures of saccharides in solution based on J couplings and the "fast sugar structure prediction software" Biomacromolecules 10 2009 3081 3088
    • (2009) Biomacromolecules , vol.10 , pp. 3081-3088
    • Xia, J.1    Margulis, C.J.2
  • 31
    • 80053332254 scopus 로고    scopus 로고
    • Searching and optimizing structure ensembles for complex flexible sugars
    • J. Xia, C.J. Margulis, and D.A. Case Searching and optimizing structure ensembles for complex flexible sugars J. Am. Chem. Soc. 133 2011 15252 15255
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 15252-15255
    • Xia, J.1    Margulis, C.J.2    Case, D.A.3
  • 32
    • 68149167531 scopus 로고    scopus 로고
    • When sugars get wet. A comprehensive study of the behavior of water on the surface of oligosaccharides
    • S.K. Ramadugu, and Y.-H. Chung C.J. Margulis When sugars get wet. A comprehensive study of the behavior of water on the surface of oligosaccharides J. Phys. Chem. B 113 2009 11003 11015
    • (2009) J. Phys. Chem. B , vol.113 , pp. 11003-11015
    • Ramadugu, S.K.1    Chung, Y.-H.2    Margulis, C.J.3
  • 34
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • N. Guex, and M.C. Peitsch SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling Electrophoresis 18 1997 2714 2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 35
    • 0001616080 scopus 로고    scopus 로고
    • Replica-exchange molecular dynamics method for protein folding
    • Y. Sugita, and Y. Okamoto Replica-exchange molecular dynamics method for protein folding Chem. Phys. Lett. 314 1999 141 151
    • (1999) Chem. Phys. Lett. , vol.314 , pp. 141-151
    • Sugita, Y.1    Okamoto, Y.2
  • 36
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple Amber force fields and development of improved protein backbone parameters
    • V. Hornak, and R. Abel C. Simmerling Comparison of multiple Amber force fields and development of improved protein backbone parameters Proteins 65 2006 712 725
    • (2006) Proteins , vol.65 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Simmerling, C.3
  • 37
    • 14244273182 scopus 로고    scopus 로고
    • Theory and applications of the generalized Born solvation model in macromolecular simulations
    • V. Tsui, and D.A. Case Theory and applications of the generalized Born solvation model in macromolecular simulations Biopolymers 56 2000-2001 275 291
    • (2000) Biopolymers , vol.56 , pp. 275-291
    • Tsui, V.1    Case, D.A.2
  • 38
    • 73449126303 scopus 로고    scopus 로고
    • Perturbation-response scanning reveals ligand entry-exit mechanisms of ferric binding protein
    • C. Atilgan, and A.R. Atilgan Perturbation-response scanning reveals ligand entry-exit mechanisms of ferric binding protein PLOS Comput. Biol. 5 2009 e1000544
    • (2009) PLOS Comput. Biol. , vol.5 , pp. 1000544
    • Atilgan, C.1    Atilgan, A.R.2
  • 39
    • 18144418170 scopus 로고    scopus 로고
    • Protein structural change upon ligand binding: Linear response theory
    • M. Ikeguchi, and J. Ueno A. Kidera Protein structural change upon ligand binding: linear response theory Phys. Rev. Lett. 94 2005 078102
    • (2005) Phys. Rev. Lett. , vol.94 , pp. 078102
    • Ikeguchi, M.1    Ueno, J.2    Kidera, A.3
  • 40
    • 84875686450 scopus 로고    scopus 로고
    • Structural dynamics flexibility informs function and evolution at a proteome scale
    • Z. Nevin Gerek, S. Kumar, and S. Banu Ozkan Structural dynamics flexibility informs function and evolution at a proteome scale Evol. Appl 6 2013 423 433
    • (2013) Evol. Appl , vol.6 , pp. 423-433
    • Nevin Gerek, Z.1    Kumar, S.2    Banu Ozkan, S.3
  • 41
    • 77952938726 scopus 로고    scopus 로고
    • Global dynamics of proteins: Bridging between structure and function
    • I. Bahar, and T.R. Lezon E. Eyal Global dynamics of proteins: bridging between structure and function Annu. Rev. Biophys 39 2010 23 42
    • (2010) Annu. Rev. Biophys , vol.39 , pp. 23-42
    • Bahar, I.1    Lezon, T.R.2    Eyal, E.3
  • 42
    • 0002098417 scopus 로고    scopus 로고
    • The development/application of a "minimalist"organic/ biochemical molecular mechanic force field using a combination of ab initio calculations and experimental data
    • P.A. Kollman, R. Dixon, W. Cornell, T. Fox, and C. Chipot et al. The development/application of a "minimalist"organic/biochemical molecular mechanic force field using a combination of ab initio calculations and experimental data Comput. Simul. Biomol. Syst. 3 1997 83 96
    • (1997) Comput. Simul. Biomol. Syst. , vol.3 , pp. 83-96
    • Kollman, P.A.1    Dixon, R.2    Cornell, W.3    Fox, T.4    Chipot, C.5
  • 43
    • 0034701222 scopus 로고    scopus 로고
    • Molecular dynamics simulations of nucleic acids with a generalized Born solvation model
    • V. Tsui, and D.A. Case Molecular dynamics simulations of nucleic acids with a generalized Born solvation model J. Am. Chem. Soc. 122 2000 2489 2498
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 2489-2498
    • Tsui, V.1    Case, D.A.2
  • 44
    • 58149094776 scopus 로고    scopus 로고
    • RosettaLigand docking with full ligand and receptor flexibility
    • I.W. Davis, and D. Baker RosettaLigand docking with full ligand and receptor flexibility J. Mol. Biol. 385 2009 381 392
    • (2009) J. Mol. Biol. , vol.385 , pp. 381-392
    • Davis, I.W.1    Baker, D.2
  • 45
    • 33750056673 scopus 로고    scopus 로고
    • ROSETTALIGAND: Protein-small molecule docking with full side-chain flexibility
    • J. Meiler, and D. Baker ROSETTALIGAND: protein-small molecule docking with full side-chain flexibility Proteins 65 2006 538 548
    • (2006) Proteins , vol.65 , pp. 538-548
    • Meiler, J.1    Baker, D.2
  • 46
    • 0036022960 scopus 로고    scopus 로고
    • Further development and validation of empirical scoring functions for structure-based binding affinity prediction
    • R. Wang, L. Lai, and S. Wang Further development and validation of empirical scoring functions for structure-based binding affinity prediction J. Comput. Aided Mol. Des. 16 2002 11 26
    • (2002) J. Comput. Aided Mol. Des. , vol.16 , pp. 11-26
    • Wang, R.1    Lai, L.2    Wang, S.3
  • 47
  • 48
    • 84880167453 scopus 로고    scopus 로고
    • Using chemical shift perturbation to characterise ligand binding
    • M.P. Williamson Using chemical shift perturbation to characterise ligand binding Prog. Nucl. Magn. Reson. Spectrosc. 73 2013 1 16
    • (2013) Prog. Nucl. Magn. Reson. Spectrosc. , vol.73 , pp. 1-16
    • Williamson, M.P.1
  • 49
    • 33845632976 scopus 로고    scopus 로고
    • Dissecting carbohydrate-Cyanovirin-N binding by structure-guided mutagenesis: Functional implications for viral entry inhibition
    • L.G. Barrientos, and E. Matei A.M. Gronenborn Dissecting carbohydrate-Cyanovirin-N binding by structure-guided mutagenesis: functional implications for viral entry inhibition Protein Eng. Des. Sel. 19 2006 525 535
    • (2006) Protein Eng. Des. Sel. , vol.19 , pp. 525-535
    • Barrientos, L.G.1    Matei, E.2    Gronenborn, A.M.3
  • 50
    • 0036113691 scopus 로고    scopus 로고
    • The domain-swapped dimer of cyanovirin-N is in a metastable folded state: Reconciliation of X-ray and NMR structures
    • L.G. Barrientos, and J.M. Louis A.M. Gronenborn The domain-swapped dimer of cyanovirin-N is in a metastable folded state: reconciliation of X-ray and NMR structures Structure 10 2002 673 686
    • (2002) Structure , vol.10 , pp. 673-686
    • Barrientos, L.G.1    Louis, J.M.2    Gronenborn, A.M.3
  • 51
    • 24644437812 scopus 로고    scopus 로고
    • The anti-HIV cyanovirin-N domain is evolutionarily conserved and occurs as a protein module in eukaryotes
    • R. Percudani, B. Montanini, and S. Ottonello The anti-HIV cyanovirin-N domain is evolutionarily conserved and occurs as a protein module in eukaryotes Proteins 60 2005 670 678
    • (2005) Proteins , vol.60 , pp. 670-678
    • Percudani, R.1    Montanini, B.2    Ottonello, S.3
  • 52
    • 84881173753 scopus 로고    scopus 로고
    • Characterizing carbohydrate-protein interactions by nuclear magnetic resonance spectroscopy
    • C.A. Bewley, and S. Shahzad-Ul-Hussan Characterizing carbohydrate-protein interactions by nuclear magnetic resonance spectroscopy Biopolymers 99 2013 796 806
    • (2013) Biopolymers , vol.99 , pp. 796-806
    • Bewley, C.A.1    Shahzad-Ul-Hussan, S.2
  • 53
    • 84870662933 scopus 로고    scopus 로고
    • Carbohydrate recognition by the antiviral lectin cyanovirin-N
    • Y.K. Fujimoto, and D.F. Green Carbohydrate recognition by the antiviral lectin cyanovirin-N J. Am. Chem. Soc. 134 2012 19639 19651
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 19639-19651
    • Fujimoto, Y.K.1    Green, D.F.2
  • 54
    • 79952498411 scopus 로고    scopus 로고
    • Crystal molecular dynamics simulations to speed up MM/PB(GB)SA evaluation of binding free energies of di-mannose deoxy analogs with P51G-m4-Cyanovirin-N
    • I.I. Vorontsov, and O. Miyashita Crystal molecular dynamics simulations to speed up MM/PB(GB)SA evaluation of binding free energies of di-mannose deoxy analogs with P51G-m4-Cyanovirin-N J. Comput. Chem. 32 2011 1043 1053
    • (2011) J. Comput. Chem. , vol.32 , pp. 1043-1053
    • Vorontsov, I.I.1    Miyashita, O.2
  • 55
    • 0038697805 scopus 로고    scopus 로고
    • Protein-protein docking predictions for the CAPRI experiment
    • J.J. Gray, and S.E. Moughon D. Baker Protein-protein docking predictions for the CAPRI experiment Proteins 52 2003 118 122
    • (2003) Proteins , vol.52 , pp. 118-122
    • Gray, J.J.1    Moughon, S.E.2    Baker, D.3
  • 56
    • 79954623874 scopus 로고    scopus 로고
    • NMR solution structure of a cyanovirin homolog from wheat head blight fungus
    • E. Matei, and J.M. Louis A.M. Gronenborn NMR solution structure of a cyanovirin homolog from wheat head blight fungus Proteins 79 2011 1538 1549
    • (2011) Proteins , vol.79 , pp. 1538-1549
    • Matei, E.1    Louis, J.M.2    Gronenborn, A.M.3
  • 57
    • 41949132916 scopus 로고    scopus 로고
    • Flexible ligand docking to multiple receptor conformations: A practical alternative
    • M. Totrov, and R. Abagyan Flexible ligand docking to multiple receptor conformations: a practical alternative Curr. Opin. Struct. Biol. 18 2008 178 184
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 178-184
    • Totrov, M.1    Abagyan, R.2
  • 58
    • 52249122794 scopus 로고    scopus 로고
    • Principles of flexible protein-protein docking
    • N. Andrusier, and E. Mashiach H.J. Wolfson Principles of flexible protein-protein docking Proteins 73 2008 271 289
    • (2008) Proteins , vol.73 , pp. 271-289
    • Andrusier, N.1    Mashiach, E.2    Wolfson, H.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.