메뉴 건너뛰기




Volumn 6, Issue , 2005, Pages

A resistant molecular dynamics and simulated annealing approach for protein homology modeling utilizing mean angles

Author keywords

[No Author keywords available]

Indexed keywords

CONSERVED RESIDUES; HOMOLOGY MODELING; PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR; PROTEIN HOMOLOGY MODELS; STANDARD DEVIATION; STRUCTURE MODELS; THREE-DIMENSIONAL STRUCTURE; X-RAY STRUCTURE;

EID: 25444446805     PISSN: 14712105     EISSN: 14712105     Source Type: Journal    
DOI: 10.1186/1471-2105-6-91     Document Type: Article
Times cited : (15)

References (61)
  • 1
    • 0034604105 scopus 로고    scopus 로고
    • A surprising simplicity to protein folding
    • Baker D: A surprising simplicity to protein folding. Nature 2000, 405:39-42.
    • (2000) Nature , vol.405 , pp. 39-42
    • Baker, D.1
  • 2
    • 0034985005 scopus 로고    scopus 로고
    • Ab initio protein structure prediction: Progress and prospects
    • Bonneau R, Baker D: Ab initio protein structure prediction: progress and prospects. Annu Rev Biophys Biomol Struct 2001, 30:173-189.
    • (2001) Annu. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 173-189
    • Bonneau, R.1    Baker, D.2
  • 4
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin AG, Brenner SE, Hubbard TJP, Chothia C: SCOP: a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 1995, 247:536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.J.P.3    Chothia, C.4
  • 6
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • Chothia C, Lesk AM: The relation between the divergence of sequence and structure in proteins. EMBO J 1986, 5:823-826.
    • (1986) EMBO J. , vol.5 , pp. 23-826
    • Chothia, C.1    Lesk, A.M.2
  • 7
    • 0026030641 scopus 로고
    • Database of homology-derived protein structures and the structural meaning of sequence alignment
    • Sander C, Schneider R: Database of homology-derived protein structures and the structural meaning of sequence alignment. Proteins 1991, 9:56-68.
    • (1991) Proteins , vol.9 , pp. 56-68
    • Sander, C.1    Schneider, R.2
  • 8
    • 0031302732 scopus 로고    scopus 로고
    • Assessment of comparative modeling in CASP2
    • Martin ACR, MacArthur MW, Thornton JM: Assessment of comparative modeling in CASP2. Proteins 1997, Suppl 1:14-28.
    • (1997) Proteins , Issue.SUPPL. 1 , pp. 14-28
    • Martin, A.C.R.1    MacArthur, M.W.2    Thornton, J.M.3
  • 13
    • 0036205337 scopus 로고    scopus 로고
    • The CATH protein family database: A resource for structural and functional annotation of genomes
    • Orengo CA, Bray JE, Buchan DW, Harrison A, Lee D, Pearl FM, et al.: The CATH protein family database: A resource for structural and functional annotation of genomes. Proteomics 2002, 2:11-21.
    • (2002) Proteomics , vol.2 , pp. 11-21
    • Orengo, C.A.1    Bray, J.E.2    Buchan, D.W.3    Harrison, A.4    Lee, D.5    Pearl, F.M.6
  • 14
    • 0029006770 scopus 로고
    • Comparison of methods for searching protein sequence databases
    • Pearson WR: Comparison of methods for searching protein sequence databases. Protein Sci 1995, 4:1145-1160.
    • (1995) Protein Sci. , vol.4 , pp. 1145-1160
    • Pearson, W.R.1
  • 17
    • 0034328688 scopus 로고    scopus 로고
    • 3D-1D threading methods for protein fold recognition
    • David R, Korenberg MJ, Hunter IW: 3D-1D threading methods for protein fold recognition. Pharmacogenomics 2000, 1:445-455.
    • (2000) Pharmacogenomics , vol.1 , pp. 445-455
    • David, R.1    Korenberg, M.J.2    Hunter, I.W.3
  • 18
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG: The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 1997, 25:4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 19
    • 0014693695 scopus 로고
    • A possible three-dimensional structure of bovine lactalbumin based on that of hen's egg-white lysosyme
    • Browne WJ, North ACT, Phillips DC, Brew K, Vanaman TC, Hill RC: A possible three-dimensional structure of bovine lactalbumin based on that of hen's egg-white lysosyme. J Mol Biol 1969, 42:65-86.
    • (1969) J. Mol. Biol. , vol.42 , pp. 65-86
    • Browne, W.J.1    North, A.C.T.2    Phillips, D.C.3    Brew, K.4    Vanaman, T.C.5    Hill, R.C.6
  • 20
    • 0023305986 scopus 로고
    • Knowledge-based prediction of protein structures and the design of novel molecules
    • Blundell TL, Sibanda BL, Sternberg MJ, Thornton JM: Knowledge-based prediction of protein structures and the design of novel molecules. Nature 1987, 326:347-352.
    • (1987) Nature , vol.326 , pp. 347-352
    • Blundell, T.L.1    Sibanda, B.L.2    Sternberg, M.J.3    Thornton, J.M.4
  • 21
    • 0025287330 scopus 로고
    • Comparative modeling methods: Application to the family of the mammalian serine proteases
    • Greer J: Comparative modeling methods: application to the family of the mammalian serine proteases. Proteins 1990, 7:317-334.
    • (1990) Proteins , vol.7 , pp. 317-334
    • Greer, J.1
  • 22
    • 0022701772 scopus 로고
    • Using known substructures in protein model building and crystallography
    • Jones TA, Thirup S: Using known substructures in protein model building and crystallography. EMBO J 1986, 5:819-822.
    • (1986) EMBO J. , vol.5 , pp. 819-822
    • Jones, T.A.1    Thirup, S.2
  • 23
    • 0024395940 scopus 로고
    • A 3D building blocks approach to analyzing and predicting structure of proteins
    • Unger R, Harel D, Wherland S, Sussman JL: A 3D building blocks approach to analyzing and predicting structure of proteins. Proteins 1989, 5:355-373.
    • (1989) Proteins , vol.5 , pp. 355-373
    • Unger, R.1    Harel, D.2    Wherland, S.3    Sussman, J.L.4
  • 24
    • 0024527223 scopus 로고
    • Modelling the polypeptide backbone with 'spare parts' from known protein structures
    • Claessens M, Van Cutsem C, Lasters I, Wodak S: Modelling the polypeptide backbone with 'spare parts' from known protein structures. Protein Eng 1989, 2:335-345.
    • (1989) Protein Eng. , vol.2 , pp. 335-345
    • Claessens, M.1    Van Cutsem, C.2    Lasters, I.3    Wodak, S.4
  • 25
    • 0026754015 scopus 로고
    • Accurate modeling of protein conformation by automatic segment matching
    • Levitt M: Accurate modeling of protein conformation by automatic segment matching. J Mol Biol 1992, 226:507-533.
    • (1992) J. Mol. Biol. , vol.226 , pp. 507-533
    • Levitt, M.1
  • 26
    • 0026018780 scopus 로고
    • A new method for building protein conformations from sequence alignments with homologues of known structure
    • Havel TF, Snow ME: A new method for building protein conformations from sequence alignments with homologues of known structure. J Mol Biol 1991, 217:7.
    • (1991) J. Mol. Biol. , vol.217 , pp. 7
    • Havel, T.F.1    Snow, M.E.2
  • 27
    • 0027510701 scopus 로고
    • An automated method for modeling proteins on known templates using distance geometry
    • Srinivasan S, March CJ, Sudarsanam S: An automated method for modeling proteins on known templates using distance geometry. Prot Sci 1993, 2:277-289.
    • (1993) Prot. Sci. , vol.2 , pp. 277-289
    • Srinivasan, S.1    March, C.J.2    Sudarsanam, S.3
  • 28
    • 0027136282 scopus 로고
    • Comparitive protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL: Comparitive protein modelling by satisfaction of spatial restraints. J Mol Biol 1993, 234:779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 29
    • 0027466730 scopus 로고
    • Prediction of the three-dimensional structures of the biotinylated domain from yeast pyruvate carboxylase and the of the lipoylated H-protein from the pea leaf glycine cleavage system: A new automated method for the prediction of protein tertiary structure
    • Brocklehurst SM, Perham RN: Prediction of the three-dimensional structures of the biotinylated domain from yeast pyruvate carboxylase and the of the lipoylated H-protein from the pea leaf glycine cleavage system: a new automated method for the prediction of protein tertiary structure. Prot Sci 1993, 2:626-639.
    • (1993) Prot. Sci. , vol.2 , pp. 626-639
    • Brocklehurst, S.M.1    Perham, R.N.2
  • 30
    • 0030322828 scopus 로고    scopus 로고
    • Homology modelling by distance geometry
    • Aszodi A, Taylor WR: Homology modelling by distance geometry. Fold Des 1996, 1:325-334.
    • (1996) Fold Des. , vol.1 , pp. 325-334
    • Aszodi, A.1    Taylor, W.R.2
  • 31
    • 0035427225 scopus 로고    scopus 로고
    • Generalized comparitive modeling (GENECOMP): A combination of sequence comparison, threading, and lattice modeling for protein structure prediction and refinement
    • Kolinski A, Betancourt MR, Kihara D, Rotkiewicz P, Skolnick J: Generalized comparitive modeling (GENECOMP): A combination of sequence comparison, threading, and lattice modeling for protein structure prediction and refinement. Proteins 2001, 44:133-149.
    • (2001) Proteins , vol.44 , pp. 133-149
    • Kolinski, A.1    Betancourt, M.R.2    Kihara, D.3    Rotkiewicz, P.4    Skolnick, J.5
  • 32
    • 0031576336 scopus 로고    scopus 로고
    • Torsion Angle Dynamics for NMR Structure Calculation with the New Program DYANA
    • Güntert P, Mumenthaler C, Wüthrich K: Torsion Angle Dynamics for NMR Structure Calculation with the New Program DYANA. J Mol Biol 1997, 273:283-298.
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 34
    • 0345280708 scopus 로고    scopus 로고
    • Determination of Mean and Standard Deviation of Dihedral Angles
    • Döker R, Maurer T, Kremer W, Neidig K-P, Kalbitzer HR: Determination of Mean and Standard Deviation of Dihedral Angles. BBRC 1999, 257:348-350.
    • (1999) BBRC , vol.257 , pp. 348-350
    • Döker, R.1    Maurer, T.2    Kremer, W.3    Neidig, K.-P.4    Kalbitzer, H.R.5
  • 35
    • 0037133641 scopus 로고    scopus 로고
    • Fold prediction of helical proteins using torsion angle dynamics and predicted restraints
    • Zhang C, Hou J, Kim S-H: Fold prediction of helical proteins using torsion angle dynamics and predicted restraints. Proc Natl Acad Sci U S A 2002, 99:3581-3585.
    • (2002) Proc. Natl. Acad. Sci. U S A , vol.99 , pp. 3581-3585
    • Zhang, C.1    Hou, J.2    Kim, S.-H.3
  • 36
    • 0028360724 scopus 로고
    • The High-resolution Structure of the Histidine-containing Phosphocarrier Protein HPr from Escherichia coli Determined by Restrained Molecular Dynamics from Nuclear Magnetic Resonance Nuclear Overhauser Effect Data
    • van Nuland NAJ, Hangyi IW, van Schaik RC, Berendsen HJ, van Gunsteren WF, Scheek RM, et al.: The High-resolution Structure of the Histidine-containing Phosphocarrier Protein HPr from Escherichia coli Determined by Restrained Molecular Dynamics from Nuclear Magnetic Resonance Nuclear Overhauser Effect Data. J Mol Biol 1994, 237:544-559.
    • (1994) J. Mol. Biol. , vol.237 , pp. 544-559
    • van Nuland, N.A.J.1    Hangyi, I.W.2    van Schaik, R.C.3    Berendsen, H.J.4    van Gunsteren, W.F.5    Scheek, R.M.6
  • 37
    • 0027340388 scopus 로고
    • The 2.0-A resolution structure of Escherichia coli histidine-containing phosphocarrier protein HPr. A redetermination
    • Jia Z, Quail JW, Waygood EB, Delbaere LT: The 2.0-A resolution structure of Escherichia coli histidine-containing phosphocarrier protein HPr. A redetermination. J Biol Chem 1993, 268:22490-22501.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22490-22501
    • Jia, Z.1    Quail, J.W.2    Waygood, E.B.3    Delbaere, L.T.4
  • 39
    • 1842486886 scopus 로고    scopus 로고
    • Automated structure determination of proteins by NMR spectroscopy
    • Gronwald W, Kalbitzer HR: Automated structure determination of proteins by NMR spectroscopy. Prog NMR Spectrosc 2004, 44:33-96.
    • (2004) Prog. NMR Spectrosc. , vol.44 , pp. 33-96
    • Gronwald, W.1    Kalbitzer, H.R.2
  • 40
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate: Carbohydrate phosphotransferase systems of bacteria
    • Postma PW, Lengeler JW, Jacobson GR: Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria. Microbiol Rev 1993, 57:543-594.
    • (1993) Microbiol. Rev. , vol.57 , pp. 543-594
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 43
    • 18244393501 scopus 로고    scopus 로고
    • Structural basis for antagonist-mediated recruitment of nuclear co-repressors by PPARalpha
    • Xu HE, Stanley TB, Montana VG, Lambert MH, Shearer BG, Cobb JE, et al.: Structural basis for antagonist-mediated recruitment of nuclear co-repressors by PPARalpha. Nature 2002, 415:813-817.
    • (2002) Nature , vol.415 , pp. 813-817
    • Xu, H.E.1    Stanley, T.B.2    Montana, V.G.3    Lambert, M.H.4    Shearer, B.G.5    Cobb, J.E.6
  • 44
    • 0035431321 scopus 로고    scopus 로고
    • Structure of the PPARalpha and -gamma ligand binding domain in complex with AZ 242; ligand selectivity and agonist activation in the PPAR family
    • Cronet P, Petersen JFW, Folmer R, Blomberg N, Sjoblom K, Karlsson U, et al.: Structure of the PPARalpha and -gamma ligand binding domain in complex with AZ 242; ligand selectivity and agonist activation in the PPAR family. Structure 2001, 9:699-706.
    • (2001) Structure , vol.9 , pp. 699-706
    • Cronet, P.1    Petersen, J.F.W.2    Folmer, R.3    Blomberg, N.4    Sjoblom, K.5    Karlsson, U.6
  • 47
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A Protein-Protein Docking Approach Based on Biochemical or Biophysical Information
    • Dominguez C, Boelens R, Bonvin AMJJ: HADDOCK: A Protein-Protein Docking Approach Based on Biochemical or Biophysical Information. J Am Chem Soc 2003, 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
  • 48
    • 0037316363 scopus 로고    scopus 로고
    • ARIA: Automated NOE assignment and NMR structure calculation
    • Linge JP, Habeck M, Rieping W, Nilges M: ARIA: automated NOE assignment and NMR structure calculation. Bioinformatics 2003, 19:315-316.
    • (2003) Bioinformatics , vol.19 , pp. 315-316
    • Linge, J.P.1    Habeck, M.2    Rieping, W.3    Nilges, M.4
  • 51
    • 0037622657 scopus 로고    scopus 로고
    • NMR-Spectroscopic Mapping of an Engineered Cavity in the I14A Mutant of HPr from Staphylococcus carnosus Using Xenon
    • Gröger C, Möglich A, Pons M, Koch B, Hengstenberg W, Kalbitzer HR, et al.: NMR-Spectroscopic Mapping of an Engineered Cavity in the I14A Mutant of HPr from Staphylococcus carnosus Using Xenon. J Am Chem Soc 2003, 125:8726-8727.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 8726-8727
    • Gröger, C.1    Möglich, A.2    Pons, M.3    Koch, B.4    Hengstenberg, W.5    Kalbitzer, H.R.6
  • 52
    • 11244296117 scopus 로고    scopus 로고
    • Solution structure of the active-centre mutant I14A of the histidine-containing phosphocarrier protein from Staphlococcus carnosus
    • Möglich A, Koch B, Gronwald W, Hengstenberg W, Brunner E, Kalbitzer HR: Solution structure of the active-centre mutant I14A of the histidine-containing phosphocarrier protein from Staphlococcus carnosus. Eur J Biochem 2004, 271:4815-4824.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 4815-4824
    • Möglich, A.1    Koch, B.2    Gronwald, W.3    Hengstenberg, W.4    Brunner, E.5    Kalbitzer, H.R.6
  • 53
    • 0030722243 scopus 로고    scopus 로고
    • Direct Measurement of Distances and Angles in Biomolecules by NMR in a Dilute Liquid Crystalline Medium
    • Tjandra NL, Bax A: Direct Measurement of Distances and Angles in Biomolecules by NMR in a Dilute Liquid Crystalline Medium. Science 1997, 278:1111-1114.
    • (1997) Science , vol.278 , pp. 1111-1114
    • Tjandra, N.L.1    Bax, A.2
  • 54
    • 0035591656 scopus 로고    scopus 로고
    • Residual dipolar couplings in protein NMR
    • Brunner E: Residual dipolar couplings in protein NMR. Concepts Magn Reson 2001, 13:238-259.
    • (2001) Concepts Magn. Reson. , vol.13 , pp. 238-259
    • Brunner, E.1
  • 55
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wüthrich K: MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graphics 1996, 14:51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 56
    • 0030623314 scopus 로고    scopus 로고
    • Relax, a Flexible Program for the Back Calculation of NOESY Spectra Based on Complete-Relaxation-Matrix Formalism
    • Görler A, Kalbitzer HR: Relax, a Flexible Program for the Back Calculation of NOESY Spectra Based on Complete-Relaxation-Matrix Formalism. J Magn Reson 1997, 124:177-188.
    • (1997) J. Magn. Reson. , vol.124 , pp. 177-188
    • Görler, A.1    Kalbitzer, H.R.2
  • 57
    • 0033090221 scopus 로고    scopus 로고
    • Computer assisted assignment of 13C or 15N edited 3D-NOESY-HSQC spectra using back calculated and experimental spectra
    • Görler A, Gronwald W, Neidig KP, Kalbitzer HR: Computer assisted assignment of 13C or 15N edited 3D-NOESY-HSQC spectra using back calculated and experimental spectra. J Magn Reson 1999, 137:39-45.
    • (1999) J. Magn. Reson. , vol.137 , pp. 39-45
    • Görler, A.1    Gronwald, W.2    Neidig, K.P.3    Kalbitzer, H.R.4
  • 58
    • 0028056155 scopus 로고
    • The 1.6 A structure of histidine-containing phosphotransfer protein HPr from Streptococcus faecalis
    • Jia Z, Vandonselaar M, Hengstenberg W, Quail JW, Delbaere LT: The 1.6 A structure of histidine-containing phosphotransfer protein HPr from Streptococcus faecalis. J Mol Biol 1994, 236:1341-1355.
    • (1994) J. Mol. Biol. , vol.236 , pp. 1341-1355
    • Jia, Z.1    Vandonselaar, M.2    Hengstenberg, W.3    Quail, J.W.4    Delbaere, L.T.5
  • 59
    • 0034829186 scopus 로고    scopus 로고
    • Three-dimensional structure of the histidine containing phosphocarrier protein (HPr) from Enterococcus faecalis in solution
    • Maurer T, Döker R, Görler A, Hengstenberg W, Kalbitzer HR: Three-dimensional structure of the histidine containing phosphocarrier protein (HPr) from Enterococcus faecalis in solution. Eur J Biochem 2001, 268:635-644.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 635-644
    • Maurer, T.1    Döker, R.2    Görler, A.3    Hengstenberg, W.4    Kalbitzer, H.R.5
  • 61
    • 0030760095 scopus 로고    scopus 로고
    • Phosphorylation on histidine is accompanied by localized structural changes in the phosphocarrier protein, HPr from Bacillus subtilis
    • Jones BE, Rajagopal P, Klevit RE: Phosphorylation on histidine is accompanied by localized structural changes in the phosphocarrier protein, HPr from Bacillus subtilis. Protein Sci 1997, 6:2107-2119.
    • (1997) Protein Sci. , vol.6 , pp. 2107-2119
    • Jones, B.E.1    Rajagopal, P.2    Klevit, R.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.