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Volumn 9, Issue 8, 2010, Pages 1784-1794

Building macromolecular assemblies by information-driven docking: Introducing the haddock multibody docking server

Author keywords

[No Author keywords available]

Indexed keywords

HOMODIMER DOUBLE STRANDED DNA; HOMOPENTAMER; HOMOTETRAMER; HOMOTRIMER; OLIGOMER; UNCLASSIFIED DRUG; AMINO ACID; MACROMOLECULE; MULTIPROTEIN COMPLEX;

EID: 77955371384     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M000051-MCP201     Document Type: Article
Times cited : (110)

References (71)
  • 3
    • 55449107518 scopus 로고    scopus 로고
    • Functional coverage of the human genome by existing structures, structural genomics targets, and homology models
    • Xie, L., and Bourne, P. E. (2005) Functional coverage of the human genome by existing structures, structural genomics targets, and homology models. PLoS Comput. Biol. 1, e31
    • (2005) PLoS Comput. Biol. , vol.1
    • Xie, L.1    Bourne, P.E.2
  • 4
    • 48749103296 scopus 로고    scopus 로고
    • Integrating diverse data for structure determination of macromolecular assemblies
    • Alber, F., Förster, F., Korkin, D., Topf, M., and Sali, A. (2008) Integrating diverse data for structure determination of macromolecular assemblies. Annu. Rev. Biochem. 77, 443-477
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 443-477
    • Alber, F.1    Förster, F.2    Korkin, D.3    Topf, M.4    Sali, A.5
  • 5
    • 35548958606 scopus 로고    scopus 로고
    • Strategies for crystallization and structure determination of very large macromolecular assemblies
    • Mueller, M., Jenni, S., and Ban, N. (2007) Strategies for crystallization and structure determination of very large macromolecular assemblies. Curr. Opin. Struct. Biol. 17, 572-579
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 572-579
    • Mueller, M.1    Jenni, S.2    Ban, N.3
  • 8
    • 33646148965 scopus 로고    scopus 로고
    • Combining NMR relaxation with chemical shift perturbation data to drive proteinprotein docking
    • van Dijk, A. D., Kaptein, R., Boelens, R., and Bonvin, A. M. (2006) Combining NMR relaxation with chemical shift perturbation data to drive proteinprotein docking. J. Biomol. NMR 34, 237-244
    • (2006) J. Biomol. NMR , vol.34 , pp. 237-244
    • Van Dijk, A.D.1    Kaptein, R.2    Boelens, R.3    Bonvin, A.M.4
  • 9
    • 23044484731 scopus 로고    scopus 로고
    • Various strategies of using residual dipolar couplings in NMR-driven protein docking: Application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data
    • van Dijk, A. D., Fushman, D., and Bonvin, A. M. (2005) Various strategies of using residual dipolar couplings in NMR-driven protein docking: application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data. Proteins 60, 367-381
    • (2005) Proteins , vol.60 , pp. 367-381
    • Van Dijk, A.D.1    Fushman, D.2    Bonvin, A.M.3
  • 10
    • 0024504877 scopus 로고
    • Receptor and antibody epitopes in human growth hormone identified by homologscanning mutagenesis
    • Cunningham, B. C., Jhurani, P., Ng, P., and Wells, J. A. (1989) Receptor and antibody epitopes in human growth hormone identified by homologscanning mutagenesis. Science 243, 1330-1336
    • (1989) Science , vol.243 , pp. 1330-1336
    • Cunningham, B.C.1    Jhurani, P.2    Ng, P.3    Wells, J.A.4
  • 11
    • 0017338248 scopus 로고
    • Chemical cross-linking: Reagents and problems in studies of membrane structure
    • Peters, K., and Richards, F. M. (1977) Chemical cross-linking: reagents and problems in studies of membrane structure. Annu. Rev. Biochem. 46, 523-551
    • (1977) Annu. Rev. Biochem. , vol.46 , pp. 523-551
    • Peters, K.1    Richards, F.M.2
  • 13
    • 0038021436 scopus 로고    scopus 로고
    • Assessment of blind predictions of protein-protein interactions: Current status of docking methods
    • Méndez, R., Leplae, R., De Maria, L., and Wodak, S. J. (2003) Assessment of blind predictions of protein-protein interactions: current status of docking methods. Proteins 52, 51-67
    • (2003) Proteins , vol.52 , pp. 51-67
    • Méndez, R.1    Leplae, R.2    De Maria, L.3    Wodak, S.J.4
  • 14
    • 0026572775 scopus 로고
    • Molecular surface recognition: Determination of geometric fit between proteins and their ligands by correlation techniques
    • Katchalski-Katzir, E., Shariv, I., Eisenstein, M., Friesem, A. A., Aflalo, C., and Vakser, I. A. (1992) Molecular surface recognition: determination of geometric fit between proteins and their ligands by correlation techniques. Proc. Natl. Acad. Sci. U.S.A. 89, 2195-2199
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 2195-2199
    • Katchalski-Katzir, E.1    Shariv, I.2    Eisenstein, M.3    Friesem, A.A.4    Aflalo, C.5    Vakser, I.A.6
  • 15
    • 0038187616 scopus 로고    scopus 로고
    • Weighted geometric docking: Incorporating external information in the rotation-translation scan
    • Ben-Zeev, E., and Eisenstein, M. (2003) Weighted geometric docking: incorporating external information in the rotation-translation scan. Proteins 52, 24-27
    • (2003) Proteins , vol.52 , pp. 24-27
    • Ben-Zeev, E.1    Eisenstein, M.2
  • 16
    • 0038583687 scopus 로고    scopus 로고
    • Protein-protein docking with a reduced protein model accounting for side-chain flexibility
    • Zacharias, M. (2003) Protein-protein docking with a reduced protein model accounting for side-chain flexibility. Protein Sci. 12, 1271-1282
    • (2003) Protein Sci. , vol.12 , pp. 1271-1282
    • Zacharias, M.1
  • 17
    • 1542316339 scopus 로고    scopus 로고
    • Rapid protein-ligand docking using soft modes from molecular dynamics simulations to account for protein deformability: Binding of FK506 to FKBP
    • Zacharias, M. (2004) Rapid protein-ligand docking using soft modes from molecular dynamics simulations to account for protein deformability: binding of FK506 to FKBP. Proteins 54, 759-767
    • (2004) Proteins , vol.54 , pp. 759-767
    • Zacharias, M.1
  • 18
    • 0038526303 scopus 로고    scopus 로고
    • ZDOCK: An initial-stage protein-docking algorithm
    • Chen, R., Li, L., and Weng, Z. (2003) ZDOCK: an initial-stage protein-docking algorithm. Proteins 52, 80-87
    • (2003) Proteins , vol.52 , pp. 80-87
    • Chen, R.1    Li, L.2    Weng, Z.3
  • 19
    • 34248513078 scopus 로고    scopus 로고
    • ZRANK: Reranking protein docking predictions with an optimized energy function
    • Pierce, B., and Weng, Z. (2007) ZRANK: reranking protein docking predictions with an optimized energy function. Proteins 67, 1078-1086
    • (2007) Proteins , vol.67 , pp. 1078-1086
    • Pierce, B.1    Weng, Z.2
  • 23
    • 34250882254 scopus 로고    scopus 로고
    • PyDock: Electrostatics and desolvation for effective scoring of rigid-body protein-protein docking
    • Cheng, T. M., Blundell, T. L., and Fernandez-Recio, J. (2007) pyDock: electrostatics and desolvation for effective scoring of rigid-body protein-protein docking. Proteins 68, 503-515
    • (2007) Proteins , vol.68 , pp. 503-515
    • Cheng, T.M.1    Blundell, T.L.2    Fernandez-Recio, J.3
  • 24
    • 33747889776 scopus 로고    scopus 로고
    • PROXIMO - A new docking algorithm to model protein complexes using data from radical probe mass spectrometry (RP-MS)
    • Gerega, S. K., and Downard, K. M. (2006) PROXIMO - a new docking algorithm to model protein complexes using data from radical probe mass spectrometry (RP-MS). Bioinformatics 22, 1702-1709
    • (2006) Bioinformatics , vol.22 , pp. 1702-1709
    • Gerega, S.K.1    Downard, K.M.2
  • 25
    • 63449125993 scopus 로고    scopus 로고
    • Inferential optimization for simultaneous fitting of multiple components into a cryoEM map of their assembly
    • Lasker, K., Topf, M., Sali, A., and Wolfson, H. J. (2009) Inferential optimization for simultaneous fitting of multiple components into a cryoEM map of their assembly. J. Mol. Biol. 388, 180-194
    • (2009) J. Mol. Biol. , vol.388 , pp. 180-194
    • Lasker, K.1    Topf, M.2    Sali, A.3    Wolfson, H.J.4
  • 27
    • 77955391393 scopus 로고    scopus 로고
    • The HADDOCK web server for data-driven biomolecular docking
    • De Vries, S. J., Van Dijk, M., and Bonvin, A. M. (2010) The HADDOCK web server for data-driven biomolecular docking. Nat. Protoc. 5, 883-897
    • (2010) Nat. Protoc. , vol.5 , pp. 883-897
    • De Vries, S.J.1    Van Dijk, M.2    Bonvin, A.M.3
  • 28
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A protein-protein docking approach based on biochemical or biophysical information
    • Dominguez, C., Boelens, R., and Bonvin, A. M. J. J. (2003) HADDOCK: a protein-protein docking approach based on biochemical or biophysical information. J. Am. Chem. Soc. 125, 1731-1737
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.J.J.3
  • 30
    • 0035800731 scopus 로고    scopus 로고
    • Osmolytes stabilize ribonuclease S by stabilizing its fragments S protein and S peptide to compact folding-competent states
    • Ratnaparkhi, G. S., and Varadarajan, R. (2001) Osmolytes stabilize ribonuclease S by stabilizing its fragments S protein and S peptide to compact folding-competent states. J. Biol. Chem. 276, 28789-28798
    • (2001) J. Biol. Chem. , vol.276 , pp. 28789-28798
    • Ratnaparkhi, G.S.1    Varadarajan, R.2
  • 31
    • 0344980718 scopus 로고    scopus 로고
    • Construction of molecular assemblies via docking: Modeling of tetramers with D2 symmetry
    • Berchanski, A., and Eisenstein, M. (2003) Construction of molecular assemblies via docking: modeling of tetramers with D2 symmetry. Proteins 53, 817-829
    • (2003) Proteins , vol.53 , pp. 817-829
    • Berchanski, A.1    Eisenstein, M.2
  • 32
    • 21644450650 scopus 로고    scopus 로고
    • Modeling oligomers with Cn or Dn symmetry: Application to CAPRI target 10
    • Berchanski, A., Segal, D., and Eisenstein, M. (2005) Modeling oligomers with Cn or Dn symmetry: application to CAPRI target 10. Proteins 60, 202-206
    • (2005) Proteins , vol.60 , pp. 202-206
    • Berchanski, A.1    Segal, D.2    Eisenstein, M.3
  • 33
    • 18844461921 scopus 로고    scopus 로고
    • Predicting oligomeric assemblies: N-mers a primer
    • Comeau, S. R., and Camacho, C. J. (2005) Predicting oligomeric assemblies: N-mers a primer. J. Struct. Biol. 150, 233-244
    • (2005) J. Struct. Biol. , vol.150 , pp. 233-244
    • Comeau, S.R.1    Camacho, C.J.2
  • 34
    • 36749048724 scopus 로고    scopus 로고
    • Prediction of the structure of symmetrical protein assemblies
    • André, I., Bradley, P., Wang, C., and Baker, D. (2007) Prediction of the structure of symmetrical protein assemblies. Proc. Natl. Acad. Sci. U.S.A. 104, 17656-17661
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 17656-17661
    • André, I.1    Bradley, P.2    Wang, C.3    Baker, D.4
  • 35
    • 17444385658 scopus 로고    scopus 로고
    • M-ZDOCK: A grid-based approach for C-n symmetric multimer docking
    • Pierce, B., Tong, W., and Weng, Z. (2005) M-ZDOCK: a grid-based approach for C-n symmetric multimer docking. Bioinformatics 21, 1472-1478
    • (2005) Bioinformatics , vol.21 , pp. 1472-1478
    • Pierce, B.1    Tong, W.2    Weng, Z.3
  • 37
    • 18844453949 scopus 로고    scopus 로고
    • Prediction of multimolecular assemblies by multiple docking
    • DOI 10.1016/j.jmb.2005.03.039, PII S0022283605003177
    • Inbar, Y., Benyamini, H., Nussinov, R., and Wolfson, H. J. (2005) Prediction of multimolecular assemblies by multiple docking. J. Mol. Biol. 349, 435-447 (Pubitemid 40693761)
    • (2005) Journal of Molecular Biology , vol.349 , Issue.2 , pp. 435-447
    • Inbar, Y.1    Benyamini, H.2    Nussinov, R.3    Wolfson, H.J.4    Honig, B.5
  • 39
    • 1542390499 scopus 로고    scopus 로고
    • Identification of protein-protein interaction sites from docking energy landscapes
    • Fernández-Recio, J., Totrov, M., and Abagyan, R. (2004) Identification of protein-protein interaction sites from docking energy landscapes. J. Mol. Biol. 335, 843-865
    • (2004) J. Mol. Biol. , vol.335 , pp. 843-865
    • Fernández-Recio, J.1    Totrov, M.2    Abagyan, R.3
  • 41
    • 0027383637 scopus 로고
    • A Calculation Strategy for the Structure Determination of Symmetrical Dimers by H-1-Nmr
    • Nilges, M. (1993) A Calculation Strategy for the Structure Determination of Symmetrical Dimers by H-1-Nmr. Proteins 17, 297-309
    • (1993) Proteins , vol.17 , pp. 297-309
    • Nilges, M.1
  • 44
    • 46249083761 scopus 로고    scopus 로고
    • Assembly reflects evolution of protein complexes
    • Levy, E. D., BoeriErba, E., Robinson, C. V., and Teichmann, S. A. (2008) Assembly reflects evolution of protein complexes. Nature 453, 1262-1265
    • (2008) Nature , vol.453 , pp. 1262-1265
    • Levy, E.D.1    BoeriErba, E.2    Robinson, C.V.3    Teichmann, S.A.4
  • 48
  • 49
    • 0035222942 scopus 로고    scopus 로고
    • Protein interaction maps for model organisms
    • Walhout, A. J., and Vidal, M. (2001) Protein interaction maps for model organisms. Nat. Rev. Mol. Cell Biol. 2, 55-62
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 55-62
    • Walhout, A.J.1    Vidal, M.2
  • 50
    • 15744373371 scopus 로고    scopus 로고
    • Proteomic approaches for generating comprehensive protein interaction maps
    • Auerbach, D., Fetchko, M., and Stagljar, I. (2003) Proteomic approaches for generating comprehensive protein interaction maps. Targets 2, 85-92
    • (2003) Targets , vol.2 , pp. 85-92
    • Auerbach, D.1    Fetchko, M.2    Stagljar, I.3
  • 58
    • 33847744247 scopus 로고    scopus 로고
    • How complete are current yeast and human protein-interaction networks?
    • Hart, G. T., Ramani, A. K., and Marcotte, E. M. (2006) How complete are current yeast and human protein-interaction networks? Genome Biol. 7, 120.1-120.9
    • (2006) Genome Biol. , vol.7
    • Hart, G.T.1    Ramani, A.K.2    Marcotte, E.M.3
  • 59
    • 0037161731 scopus 로고    scopus 로고
    • Comparative assessment of large-scale data sets of protein-protein interactions
    • von Mering, C., Krause, R., Snel, B., Cornell, M., Oliver, S. G., Fields, S., and Bork, P. (2002) Comparative assessment of large-scale data sets of protein-protein interactions. Nature 417, 399-403
    • (2002) Nature , vol.417 , pp. 399-403
    • Von Mering, C.1    Krause, R.2    Snel, B.3    Cornell, M.4    Oliver, S.G.5    Fields, S.6    Bork, P.7
  • 61
    • 33750113344 scopus 로고    scopus 로고
    • The elusive yeast interactome
    • Goll, J., and Uetz, P. (2006) The elusive yeast interactome. Genome Biol. 7, 223.1-223.6
    • (2006) Genome Biol. , vol.7
    • Goll, J.1    Uetz, P.2
  • 62
    • 77952068704 scopus 로고    scopus 로고
    • Are scoring functions in protein protein docking ready to predict interactomes? Clues from a novel binding affinity benchmark
    • in press
    • Kastritis, P. L., and Bonvin, A. M. J. J. (2010) Are scoring functions in protein protein docking ready to predict interactomes? Clues from a novel binding affinity benchmark. J. Proteome Res., in press
    • (2010) J. Proteome Res.
    • Kastritis, P.L.1    Bonvin, A.M.J.J.2
  • 63
    • 33749077506 scopus 로고    scopus 로고
    • Prediction of protein-protein interaction based on structure
    • Fernandez-Ballester, G., and Serrano, L. (2006) Prediction of protein-protein interaction based on structure. Methods Mol. Biol. 340, 207-234
    • (2006) Methods Mol. Biol. , vol.340 , pp. 207-234
    • Fernandez-Ballester, G.1    Serrano, L.2
  • 65
    • 43349101236 scopus 로고    scopus 로고
    • MTMDAT: Automated analysis and visualization of mass spectrometry data for tertiary and quaternary structure probing of proteins
    • Hennig, J., Hennig, K. D., and Sunnerhagen, M. (2008) MTMDAT: automated analysis and visualization of mass spectrometry data for tertiary and quaternary structure probing of proteins. Bioinformatics 24, 1310-1312
    • (2008) Bioinformatics , vol.24 , pp. 1310-1312
    • Hennig, J.1    Hennig, K.D.2    Sunnerhagen, M.3
  • 66
    • 0032725980 scopus 로고    scopus 로고
    • A test case for structure-based functional assignment: The 1.2 angstrom crystal structure of the yjgF gene product from Escherichia coli
    • Volz, K. (1999) A test case for structure-based functional assignment: the 1.2 angstrom crystal structure of the yjgF gene product from Escherichia coli. Protein Sci. 8, 2428-2437
    • (1999) Protein Sci. , vol.8 , pp. 2428-2437
    • Volz, K.1
  • 68
    • 0042667040 scopus 로고    scopus 로고
    • Structural basis of carbohydrate recognition by the lectin LecB from Pseudomonas aeruginosa
    • Loris, R., Tielker, D., Jaeger, K. E., and Wyns, L. (2003) Structural basis of carbohydrate recognition by the lectin LecB from Pseudomonas aeruginosa. J. Mol. Biol. 331, 861-870
    • (2003) J. Mol. Biol. , vol.331 , pp. 861-870
    • Loris, R.1    Tielker, D.2    Jaeger, K.E.3    Wyns, L.4
  • 70
    • 0030839256 scopus 로고    scopus 로고
    • High-resolution structure of a polyomavirus VP1-oligosaccharide complex: Implications for assembly and receptor binding
    • Stehle, T., and Harrison, S. C. (1997) High-resolution structure of a polyomavirus VP1-oligosaccharide complex: implications for assembly and receptor binding. EMBO J. 16, 5139-5148
    • (1997) EMBO J. , vol.16 , pp. 5139-5148
    • Stehle, T.1    Harrison, S.C.2
  • 71
    • 0025878205 scopus 로고
    • The phage-434 Cro/Or1 complex at 2.5Å resolution
    • Mondragón, A., and Harrison, S. C. (1991) The phage-434 Cro/Or1 complex at 2.5Å resolution. J. Mol. Biol. 219, 321-334
    • (1991) J. Mol. Biol. , vol.219 , pp. 321-334
    • Mondragón, A.1    Harrison, S.C.2


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