메뉴 건너뛰기




Volumn 335, Issue 3, 2004, Pages 843-865

Identification of protein-protein interaction sites from docking energy landscapes

Author keywords

Binding site identification; Docking energy landscapes; Hot spots; ICM, internal coordinate mechanics; PDB, Protein Data Bank; PPI, protein protein interaction; Protein protein interactions; Pseudo Brownian Monte Carlo; RMSD, root mean square deviation

Indexed keywords

PROTEIN;

EID: 1542390499     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.10.069     Document Type: Article
Times cited : (244)

References (59)
  • 2
    • 0036468396 scopus 로고    scopus 로고
    • Protein-protein association kinetics and protein docking
    • Camacho C.J., Vajda S. Protein-protein association kinetics and protein docking. Curr. Opin. Struct. Biol. 12:2002;36-40.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 36-40
    • Camacho, C.J.1    Vajda, S.2
  • 3
    • 0035281357 scopus 로고    scopus 로고
    • Computer simulation of protein-protein interactions
    • Elcock A.H., Sept D., McCammon J.A. Computer simulation of protein-protein interactions. J. Phys. Chem. ser. B. 105:2001;1504-1518.
    • (2001) J. Phys. Chem. Ser. B , vol.105 , pp. 1504-1518
    • Elcock, A.H.1    Sept, D.2    McCammon, J.A.3
  • 4
    • 0036149480 scopus 로고    scopus 로고
    • Soft protein-protein docking in internal coordinates
    • Fernandez-Recio J., Totrov M., Abagyan R. Soft protein-protein docking in internal coordinates. Protein Sci. 11:2002;280-291.
    • (2002) Protein Sci. , vol.11 , pp. 280-291
    • Fernandez-Recio, J.1    Totrov, M.2    Abagyan, R.3
  • 5
    • 0036468385 scopus 로고    scopus 로고
    • Prediction of protein-protein interactions by docking methods
    • Smith G.R., Sternberg M.J. Prediction of protein-protein interactions by docking methods. Curr. Opin. Struct. Biol. 12:2002;28-35.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 28-35
    • Smith, G.R.1    Sternberg, M.J.2
  • 6
  • 7
    • 0018165127 scopus 로고
    • Computer analysis of protein-protein interaction
    • Wodak S.J., Janin J. Computer analysis of protein-protein interaction. J. Mol. Biol. 124:1978;323-342.
    • (1978) J. Mol. Biol. , vol.124 , pp. 323-342
    • Wodak, S.J.1    Janin, J.2
  • 8
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan A.A., Thorn K.S. Anatomy of hot spots in protein interfaces. J. Mol. Biol. 280:1998;1-9.
    • (1998) J. Mol. Biol. , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 9
    • 0032540358 scopus 로고    scopus 로고
    • Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity
    • Clackson T., Ultsch M.H., Wells J.A., de Vos A.M. Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity. J. Mol. Biol. 277:1998;1111-1128.
    • (1998) J. Mol. Biol. , vol.277 , pp. 1111-1128
    • Clackson, T.1    Ultsch, M.H.2    Wells, J.A.3    De Vos, A.M.4
  • 10
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson T., Wells J.A. A hot spot of binding energy in a hormone-receptor interface. Science. 267:1995;383-386.
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 11
  • 12
    • 0024362070 scopus 로고
    • On the attribution of binding energy in antigen-antibody complexes McPC 603, D1.3, and HyHEL-5
    • Novotny J., Bruccoleri R.E., Saul F.A. On the attribution of binding energy in antigen-antibody complexes McPC 603, D1.3, and HyHEL-5. Biochemistry. 28:1989;4735-4749.
    • (1989) Biochemistry , vol.28 , pp. 4735-4749
    • Novotny, J.1    Bruccoleri, R.E.2    Saul, F.A.3
  • 13
    • 0024046505 scopus 로고
    • An investigation of protein subunit and domain interfaces
    • Argos P. An investigation of protein subunit and domain interfaces. Protein Eng. 2:1988;101-113.
    • (1988) Protein Eng. , vol.2 , pp. 101-113
    • Argos, P.1
  • 15
    • 0024246956 scopus 로고
    • Surface, subunit interfaces and interior of oligomeric proteins
    • Janin J., Miller S., Chothia C. Surface, subunit interfaces and interior of oligomeric proteins. J. Mol. Biol. 204:1988;155-164.
    • (1988) J. Mol. Biol. , vol.204 , pp. 155-164
    • Janin, J.1    Miller, S.2    Chothia, C.3
  • 16
    • 0029109468 scopus 로고
    • Protein-protein interactions: A review of protein dimer structures
    • Jones S., Thornton J.M. Protein-protein interactions: a review of protein dimer structures. Prog. Biophys. Mol. Biol. 63:1995;31-65.
    • (1995) Prog. Biophys. Mol. Biol. , vol.63 , pp. 31-65
    • Jones, S.1    Thornton, J.M.2
  • 17
  • 18
    • 0031565729 scopus 로고    scopus 로고
    • Analysis of protein-protein interaction sites using surface patches
    • Jones S., Thornton J.M. Analysis of protein-protein interaction sites using surface patches. J. Mol. Biol. 272:1997;121-132.
    • (1997) J. Mol. Biol. , vol.272 , pp. 121-132
    • Jones, S.1    Thornton, J.M.2
  • 19
    • 0028332007 scopus 로고
    • A role for surface hydrophobicity in protein-protein recognition
    • Young L., Jernigan R.L., Covell D.G. A role for surface hydrophobicity in protein-protein recognition. Protein Sci. 3:1994;717-729.
    • (1994) Protein Sci. , vol.3 , pp. 717-729
    • Young, L.1    Jernigan, R.L.2    Covell, D.G.3
  • 20
    • 0016708122 scopus 로고
    • Principles of protein-protein recognition
    • Chothia C., Janin J. Principles of protein-protein recognition. Nature. 256:1975;705-708.
    • (1975) Nature , vol.256 , pp. 705-708
    • Chothia, C.1    Janin, J.2
  • 21
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Conte L.L., Chothia C., Janin J. The atomic structure of protein-protein recognition sites. J. Mol. Biol. 285:1999;2177-2198.
    • (1999) J. Mol. Biol. , vol.285 , pp. 2177-2198
    • Conte, L.L.1    Chothia, C.2    Janin, J.3
  • 22
    • 0025123333 scopus 로고
    • The structure of protein-protein recognition sites
    • Janin J., Chothia C. The structure of protein-protein recognition sites. J. Biol. Chem. 265:1990;16027-16030.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16027-16030
    • Janin, J.1    Chothia, C.2
  • 23
    • 0036306236 scopus 로고    scopus 로고
    • On the role of electrostatic interactions in the design of protein-protein interfaces
    • Sheinerman F.B., Honig B. On the role of electrostatic interactions in the design of protein-protein interfaces. J. Mol. Biol. 318:2002;161-177.
    • (2002) J. Mol. Biol. , vol.318 , pp. 161-177
    • Sheinerman, F.B.1    Honig, B.2
  • 24
    • 0031565725 scopus 로고    scopus 로고
    • Prediction of protein-protein interaction sites using patch analysis
    • Jones S., Thornton J.M. Prediction of protein-protein interaction sites using patch analysis. J. Mol. Biol. 272:1997;133-143.
    • (1997) J. Mol. Biol. , vol.272 , pp. 133-143
    • Jones, S.1    Thornton, J.M.2
  • 25
    • 0035882570 scopus 로고    scopus 로고
    • Prediction of protein interaction sites from sequence profile and residue neighbor list
    • Zhou H.X., Shan Y. Prediction of protein interaction sites from sequence profile and residue neighbor list. Proteins: Struct. Funct. Genet. 44:2001;336-343.
    • (2001) Proteins: Struct. Funct. Genet. , vol.44 , pp. 336-343
    • Zhou, H.X.1    Shan, Y.2
  • 26
    • 0035830963 scopus 로고    scopus 로고
    • Protein-protein association: Investigation of factors influencing association rates by Brownian dynamics simulations
    • Gabdoulline R.R., Wade R.C. Protein-protein association: investigation of factors influencing association rates by Brownian dynamics simulations. J. Mol. Biol. 306:2001;1139-1155.
    • (2001) J. Mol. Biol. , vol.306 , pp. 1139-1155
    • Gabdoulline, R.R.1    Wade, R.C.2
  • 27
    • 0031010107 scopus 로고    scopus 로고
    • The kinetics of protein-protein recognition
    • Janin J. The kinetics of protein-protein recognition. Proteins: Struct. Funct. Genet. 28:1997;153-161.
    • (1997) Proteins: Struct. Funct. Genet. , vol.28 , pp. 153-161
    • Janin, J.1
  • 29
    • 0033587727 scopus 로고    scopus 로고
    • A systematic study of low-resolution recognition in protein-protein complexes
    • Vakser I.A., Matar O.G., Lam C.F. A systematic study of low-resolution recognition in protein-protein complexes. Proc. Natl Acad. Sci. USA. 96:1999;8477-8482.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 8477-8482
    • Vakser, I.A.1    Matar, O.G.2    Lam, C.F.3
  • 30
    • 0036369841 scopus 로고    scopus 로고
    • Screened charge electrostatic model in protein-protein docking simulations
    • Fernandez-Recio J., Totrov M., Abagyan R. Screened charge electrostatic model in protein-protein docking simulations. Pac. Symp. Biocomput. 7:2002;552-565.
    • (2002) Pac. Symp. Biocomput. , vol.7 , pp. 552-565
    • Fernandez-Recio, J.1    Totrov, M.2    Abagyan, R.3
  • 31
    • 0028102849 scopus 로고
    • Effect of conformational flexibility and solvation on receptor-ligand binding free energies
    • Vajda S., Weng Z., Rosenfeld R., DeLisi C. Effect of conformational flexibility and solvation on receptor-ligand binding free energies. Biochemistry. 33:1994;13977-13988.
    • (1994) Biochemistry , vol.33 , pp. 13977-13988
    • Vajda, S.1    Weng, Z.2    Rosenfeld, R.3    Delisi, C.4
  • 32
    • 0024084758 scopus 로고
    • A rapid method of calculating charge-charge interaction energies in proteins
    • Pickersgill R.W. A rapid method of calculating charge-charge interaction energies in proteins. Protein Eng. 2:1988;247-248.
    • (1988) Protein Eng. , vol.2 , pp. 247-248
    • Pickersgill, R.W.1
  • 34
    • 0036070661 scopus 로고    scopus 로고
    • Interatomic potentials and solvation parameters from protein engineering data for buried residues
    • Lomize A.L., Riebarkh M.Y., Pogozheva I.D. Interatomic potentials and solvation parameters from protein engineering data for buried residues. Protein Sci. 11:2002;1984-2000.
    • (2002) Protein Sci. , vol.11 , pp. 1984-2000
    • Lomize, A.L.1    Riebarkh, M.Y.2    Pogozheva, I.D.3
  • 35
    • 0032800328 scopus 로고    scopus 로고
    • Electrostatic forces involved in orienting Anabaena ferredoxin during binding to Anabaena ferredoxin:NADP+reductase: Site-specific mutagenesis, transient kinetic measurements, and electrostatic surface potentials
    • Hurley J.K., Hazzard J.T., Martinez-Julvez M., Medina M., Gomez-Moreno C., Tollin G. Electrostatic forces involved in orienting Anabaena ferredoxin during binding to Anabaena ferredoxin:NADP+reductase: site-specific mutagenesis, transient kinetic measurements, and electrostatic surface potentials. Protein Sci. 8:1999;1614-1622.
    • (1999) Protein Sci. , vol.8 , pp. 1614-1622
    • Hurley, J.K.1    Hazzard, J.T.2    Martinez-Julvez, M.3    Medina, M.4    Gomez-Moreno, C.5    Tollin, G.6
  • 36
    • 0030041323 scopus 로고    scopus 로고
    • Dimerization of the extracellular domain of the erythropoietin (EPO) receptor by EPO: One high-affinity and one low-affinity interaction
    • Philo J.S., Aoki K.H., Arakawa T., Narhi L.O., Wen J. Dimerization of the extracellular domain of the erythropoietin (EPO) receptor by EPO: one high-affinity and one low-affinity interaction. Biochemistry. 35:1996;1681-1691.
    • (1996) Biochemistry , vol.35 , pp. 1681-1691
    • Philo, J.S.1    Aoki, K.H.2    Arakawa, T.3    Narhi, L.O.4    Wen, J.5
  • 38
    • 0033618555 scopus 로고    scopus 로고
    • Detecting protein function and protein-protein interactions from genome sequences
    • Marcotte E.M., Pellegrini M., Ng H.L., Rice D.W., Yeates T.O., Eisenberg D. Detecting protein function and protein-protein interactions from genome sequences. Science. 285:1999;751-753.
    • (1999) Science , vol.285 , pp. 751-753
    • Marcotte, E.M.1    Pellegrini, M.2    Ng, H.L.3    Rice, D.W.4    Yeates, T.O.5    Eisenberg, D.6
  • 39
    • 0021871375 scopus 로고
    • A computational procedure for determining energetically favorable binding sites on biologically important macromolecules
    • Goodford P.J. A computational procedure for determining energetically favorable binding sites on biologically important macromolecules. J. Med. Chem. 28:1985;849-857.
    • (1985) J. Med. Chem. , vol.28 , pp. 849-857
    • Goodford, P.J.1
  • 40
    • 0031302358 scopus 로고    scopus 로고
    • Flexible protein-ligand docking by global energy optimization in internal coordinates
    • Totrov M., Abagyan R. Flexible protein-ligand docking by global energy optimization in internal coordinates. Proteins: Struct. Funct. Genet. Suppl. 1:1997;215-220.
    • (1997) Proteins: Struct. Funct. Genet. Suppl , vol.1 , pp. 215-220
    • Totrov, M.1    Abagyan, R.2
  • 42
    • 0022596727 scopus 로고
    • Solvation energy in protein folding and binding
    • Eisenberg D., McLachlan A.D. Solvation energy in protein folding and binding. Nature. 319:1986;199-203.
    • (1986) Nature , vol.319 , pp. 199-203
    • Eisenberg, D.1    McLachlan, A.D.2
  • 43
    • 0027080909 scopus 로고
    • Atomic solvation parameters applied to molecular dynamics of proteins in solution
    • Wesson L., Eisenberg D. Atomic solvation parameters applied to molecular dynamics of proteins in solution. Protein Sci. 1:1992;227-235.
    • (1992) Protein Sci. , vol.1 , pp. 227-235
    • Wesson, L.1    Eisenberg, D.2
  • 44
    • 0000538967 scopus 로고    scopus 로고
    • Protein structure prediction by global energy optimization
    • van Gunsteren W.F. et al. Dordrecht: Kluwer Academic Publisher
    • Abagyan R. Protein structure prediction by global energy optimization. van Gunsteren W.F., et al. Computer Simulations of Biomolecular Systems. vol. 3:1997;363-394 Kluwer Academic Publisher, Dordrecht.
    • (1997) Computer Simulations of Biomolecular Systems , vol.3 , pp. 363-394
    • Abagyan, R.1
  • 46
    • 33845374932 scopus 로고
    • Ionization potentials and electron affinities in aqueous solution
    • Pearson R.G. Ionization potentials and electron affinities in aqueous solution. J. Am. Chem. Soc. 108:1986;6109-6114.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 6109-6114
    • Pearson, R.G.1
  • 47
    • 84986522918 scopus 로고
    • ICM: A new method for structure modeling and design: Applications to docking and structure prediction from the distorted native conformation
    • Abagyan R., Totrov M., Kuznetsov D. ICM: a new method for structure modeling and design: applications to docking and structure prediction from the distorted native conformation. J. Comput. Chem. 15:1994;488-506.
    • (1994) J. Comput. Chem. , vol.15 , pp. 488-506
    • Abagyan, R.1    Totrov, M.2    Kuznetsov, D.3
  • 48
    • 0007888889 scopus 로고    scopus 로고
    • San Diego: MolSoft LLC
    • MolSoft. ICM 2.8 Program Manual. 2000;MolSoft LLC, San Diego.
    • (2000) ICM 2.8 Program Manual
  • 50
    • 0026681839 scopus 로고
    • Optimal protocol and trajectory visualization for conformational searches of peptides and proteins
    • Abagyan R., Argos P. Optimal protocol and trajectory visualization for conformational searches of peptides and proteins. J. Mol. Biol. 225:1992;519-532.
    • (1992) J. Mol. Biol. , vol.225 , pp. 519-532
    • Abagyan, R.1    Argos, P.2
  • 51
    • 0000484499 scopus 로고
    • Hydrophobic parameters-pi of amino-acid side-chains from the partitioning of N-acetyl-amino-acid amides
    • Fauchere J.L., Pliska V. Hydrophobic parameters-pi of amino-acid side-chains from the partitioning of N-acetyl-amino-acid amides. Eur. J. Med. Chem. 18:1983;369-375.
    • (1983) Eur. J. Med. Chem. , vol.18 , pp. 369-375
    • Fauchere, J.L.1    Pliska, V.2
  • 52
    • 0000238336 scopus 로고
    • A simplex method for function minimization
    • Nelder J.A., Mead R. A simplex method for function minimization. Comput. J. 7:1965;308-313.
    • (1965) Comput. J. , vol.7 , pp. 308-313
    • Nelder, J.A.1    Mead, R.2
  • 53
    • 0021209611 scopus 로고
    • Electron transfer by ferredoxin:NADP+reductase. Rapid-reaction evidence for participation of a ternary complex
    • Batie C.J., Kamin H. Electron transfer by ferredoxin:NADP+reductase. Rapid-reaction evidence for participation of a ternary complex. J. Biol. Chem. 259:1984;11976-11985.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11976-11985
    • Batie, C.J.1    Kamin, H.2
  • 54
  • 55
    • 0032188942 scopus 로고    scopus 로고
    • Efficiency of signalling through cytokine receptors depends critically on receptor orientation
    • Syed R.S., Reid S.W., Li C., Cheetham J.C., Aoki K.H., Liu B., et al. Efficiency of signalling through cytokine receptors depends critically on receptor orientation. Nature. 395:1998;511-516.
    • (1998) Nature , vol.395 , pp. 511-516
    • Syed, R.S.1    Reid, S.W.2    Li, C.3    Cheetham, J.C.4    Aoki, K.H.5    Liu, B.6
  • 56
    • 17344380633 scopus 로고    scopus 로고
    • ICM-DISCO docking by global energy optimization with fully flexible side-chains
    • Fernandez-Recio J., Totrov M., Abagyan R. ICM-DISCO docking by global energy optimization with fully flexible side-chains. Proteins: Struct. Funct. Genet. 52:2003;113-117.
    • (2003) Proteins: Struct. Funct. Genet. , vol.52 , pp. 113-117
    • Fernandez-Recio, J.1    Totrov, M.2    Abagyan, R.3
  • 57
    • 0026801518 scopus 로고
    • Molecular structure of the acyl-enzyme intermediate in beta-lactam hydrolysis at 1.7 Å resolution
    • Strynadka N.C., Adachi H., Jensen S.E., Johns K., Sielecki A., Betzel C., et al. Molecular structure of the acyl-enzyme intermediate in beta-lactam hydrolysis at 1.7 Å resolution. Nature. 359:1992;700-705.
    • (1992) Nature , vol.359 , pp. 700-705
    • Strynadka, N.C.1    Adachi, H.2    Jensen, S.E.3    Johns, K.4    Sielecki, A.5    Betzel, C.6
  • 58
    • 0029949210 scopus 로고    scopus 로고
    • A potent new mode of beta-lactamase inhibition revealed by the 1.7 Å X-ray crystallographic structure of the TEM-1-BLIP complex
    • Strynadka N.C., Jensen S.E., Alzari P.M., James M.N. A potent new mode of beta-lactamase inhibition revealed by the 1.7 Å X-ray crystallographic structure of the TEM-1-BLIP complex. Nature Struct. Biol. 3:1996;290-297.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 290-297
    • Strynadka, N.C.1    Jensen, S.E.2    Alzari, P.M.3    James, M.N.4
  • 59
    • 0028287903 scopus 로고
    • Structural and kinetic characterization of a beta-lactamase-inhibitor protein
    • Strynadka N.C., Jensen S.E., Johns K., Blanchard H., Page M., Matagne A., et al. Structural and kinetic characterization of a beta-lactamase-inhibitor protein. Nature. 368:1994;657-660.
    • (1994) Nature , vol.368 , pp. 657-660
    • Strynadka, N.C.1    Jensen, S.E.2    Johns, K.3    Blanchard, H.4    Page, M.5    Matagne, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.