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Volumn 271, Issue 4, 1997, Pages 511-523

Correlated mutations contain information about protein - protein interaction

Author keywords

Co adaptation; Correlated mutations; Docking; Hsc70; Protein contacts

Indexed keywords

HEAT SHOCK PROTEIN 70; HEMOGLOBIN; PROTEIN;

EID: 0030821675     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1198     Document Type: Article
Times cited : (448)

References (54)
  • 1
    • 0023660022 scopus 로고
    • Correlation of co-ordinated amino acid substitutions with function in viruses related to tobacco mosaic virus
    • Altschuh D., Lesk A. M., Bloomer A. C., Klug A. Correlation of co-ordinated amino acid substitutions with function in viruses related to tobacco mosaic virus. J. Mol. Biol. 193:1987;693-707.
    • (1987) J. Mol. Biol. , vol.193 , pp. 693-707
    • Altschuh, D.1    Lesk, A.M.2    Bloomer, A.C.3    Klug, A.4
  • 2
    • 0024084164 scopus 로고
    • Coordinated amino acid changes in homologous protein families
    • Altschuh D., Vernet T., Berti P., Moras D., Nagai K. Coordinated amino acid changes in homologous protein families. Protein Eng. 2:1988;193-199.
    • (1988) Protein Eng. , vol.2 , pp. 193-199
    • Altschuh, D.1    Vernet, T.2    Berti, P.3    Moras, D.4    Nagai, K.5
  • 3
    • 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
  • 4
    • 0030855390 scopus 로고    scopus 로고
    • ESCHER: A new docking procedure applied to the reconstruction of protein tertiary structure
    • Ausiello G., Cesareni G., Helmer-Citterich M. ESCHER: a new docking procedure applied to the reconstruction of protein tertiary structure. Proteins: Struct. Funct. Genet. In the press:1997.
    • (1997) Proteins: Struct. Funct. Genet
    • Ausiello, G.1    Cesareni, G.2    Helmer-Citterich, M.3
  • 5
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2.2 Å resolution
    • Babu Y. S., Bugg C. E., Cook W. J. Structure of calmodulin refined at 2.2 Å resolution. J. Mol. Biol. 204:1988;191-204.
    • (1988) J. Mol. Biol. , vol.204 , pp. 191-204
    • Babu, Y.S.1    Bugg, C.E.2    Cook, W.J.3
  • 6
    • 0028865843 scopus 로고
    • 3D domain swapping: A mechanism for oligomer assembly
    • Bennett M. J., Schlunegger M. P., Eisenberg D. 3D domain swapping: a mechanism for oligomer assembly. Protein Sci. 4:1995;2455-2468.
    • (1995) Protein Sci. , vol.4 , pp. 2455-2468
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 10
    • 0029025913 scopus 로고
    • A geometry-based suite of molecular docking processes
    • Fischer D., Lin S. L., Wolfson H. L., Nussinov R. A geometry-based suite of molecular docking processes. J. Mol. Biol. 248:1995;459-477.
    • (1995) J. Mol. Biol. , vol.248 , pp. 459-477
    • Fischer, D.1    Lin, S.L.2    Wolfson, H.L.3    Nussinov, R.4
  • 11
    • 0025100372 scopus 로고
    • Three-dimensional structure of the ATPase fragment of a 70 K heat shock cognate protein
    • Flaherty K. M., DeLuca-Flaherty C., McKay D. B. Three-dimensional structure of the ATPase fragment of a 70 K heat shock cognate protein. Nature. 346:1990;623-628.
    • (1990) Nature , vol.346 , pp. 623-628
    • Flaherty, K.M.1    Deluca-Flaherty, C.2    McKay, D.B.3
  • 15
    • 0027211894 scopus 로고
    • Additivity of mutant effects assessed by binomial mutagenesis
    • Gregoret L. M., Sauer R. T. Additivity of mutant effects assessed by binomial mutagenesis. Proc. Natl Acad. Sci. USA, 90:1993;4246-4250.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 4246-4250
    • Gregoret, L.M.1    Sauer, R.T.2
  • 16
    • 0027958638 scopus 로고
    • PUZZLE: A new method for automated protein docking based on surface shape complementarity
    • Helmer-Citterich M., Tramontano A. PUZZLE: a new method for automated protein docking based on surface shape complementarity. J. Mol. Biol. 235:1994;1021-1031.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1021-1031
    • Helmer-Citterich, M.1    Tramontano, A.2
  • 18
    • 0026536335 scopus 로고
    • Solution structure of a calmodulin-target peptide complex by multidimensional NMR
    • Ikura M., Clore G. M., Gronenborn A. M., Zhu G., Klee C. B. Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science. 256:1992;632-638.
    • (1992) Science , vol.256 , pp. 632-638
    • Ikura, M.1    Clore, G.M.2    Gronenborn, A.M.3    Zhu, G.4    Klee, C.B.5
  • 19
    • 0029019869 scopus 로고
    • A continuum model for protein-protein interactions: Application to the docking problem
    • Jackson R. M., Sternberg M. J. E. A continuum model for protein-protein interactions: application to the docking problem. J. Mol. Biol. 250:1995;258-275.
    • (1995) J. Mol. Biol. , vol.250 , pp. 258-275
    • Jackson, R.M.1    Sternberg, M.J.E.2
  • 20
    • 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
  • 21
    • 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
  • 22
    • 0028799067 scopus 로고
    • Hemoglobin allostery: Resonance raman spectroscopy of kinetic intermediates
    • Jayaraman V., Rodgers K. R., Mukerji I., Spiro T. G. Hemoglobin allostery: resonance raman spectroscopy of kinetic intermediates. Science. 269:1995;1843-1848.
    • (1995) Science , vol.269 , pp. 1843-1848
    • Jayaraman, V.1    Rodgers, K.R.2    Mukerji, I.3    Spiro, T.G.4
  • 23
    • 0026310932 scopus 로고
    • "soft docking": Matching of molecular surface cubes
    • Jiang F., Kim S. H. "Soft docking": matching of molecular surface cubes. J. Mol. Biol. 219:1991;79-102.
    • (1991) J. Mol. Biol. , vol.219 , pp. 79-102
    • Jiang, F.1    Kim, S.H.2
  • 24
  • 25
    • 0026695805 scopus 로고
    • High-resolution X-Ray study of deoxyhemoglobin Rothschild 37 beta TRP→ARG : A mutation that creates an intersubunit chloride-binding site
    • Kavanaugh J. S., Rogers P. H., Case D. A., Arnone A. High-resolution X-Ray study of deoxyhemoglobin Rothschild 37 beta TRP→ARG : a mutation that creates an intersubunit chloride-binding site. Biochemistry. 31:1992;4111-4121.
    • (1992) Biochemistry , vol.31 , pp. 4111-4121
    • Kavanaugh, J.S.1    Rogers, P.H.2    Case, D.A.3    Arnone, A.4
  • 27
    • 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., Friesen A., Aflalo C., Vakser I. Molecular surface recognition: determination of geometric fit between proteins and their ligands by correlation techniques. Proc. Natl Acad. Sci. USA. 89:1992;2195-2199.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 2195-2199
    • Katchalski-Katzir, E.1    Shariv, I.2    Eisenstein, M.3    Friesen, A.4    Aflalo, C.5    Vakser, I.6
  • 28
    • 0029902763 scopus 로고    scopus 로고
    • Methods for predicting molecular complexes involving proteins
    • Lengauer T., Rarey M. Methods for predicting molecular complexes involving proteins. Curr. Opin. Struct. Biol. 5:1996;402-406.
    • (1996) Curr. Opin. Struct. Biol. , vol.5 , pp. 402-406
    • Lengauer, T.1    Rarey, M.2
  • 29
    • 0019332167 scopus 로고
    • How different amino acid sequences determine similar protein structures: The structure and evolutionary dynamics of the globins
    • Lesk A. M., Chothia C. How different amino acid sequences determine similar protein structures: the structure and evolutionary dynamics of the globins. J. Mol. Biol. 136:1980;225-270.
    • (1980) J. Mol. Biol. , vol.136 , pp. 225-270
    • Lesk, A.M.1    Chothia, C.2
  • 30
    • 0029013908 scopus 로고
    • The role of ATP in the functional cycle of the DnaK chaperone system
    • McCarty J. S., Buchberger A., Reinstein J., Bukau B. The role of ATP in the functional cycle of the DnaK chaperone system. J. Mol. Biol. 249:1995;126-137.
    • (1995) J. Mol. Biol. , vol.249 , pp. 126-137
    • McCarty, J.S.1    Buchberger, A.2    Reinstein, J.3    Bukau, B.4
  • 31
    • 0015243774 scopus 로고
    • Test for comparing related amino acid sequences
    • McLachlan A. D. Test for comparing related amino acid sequences. J. Mol. Biol. 61:1971;409-424.
    • (1971) J. Mol. Biol. , vol.61 , pp. 409-424
    • McLachlan, A.D.1
  • 32
    • 0027172465 scopus 로고
    • Thermodinamic and structural analysis of the folding/unfolding transitions of the Escherichia coli molecular chaperone DnaK
    • Montgomery D., Jordan R., McMacken R., Freire E. Thermodinamic and structural analysis of the folding/unfolding transitions of the Escherichia coli molecular chaperone DnaK. J. Mol. Biol. 232:1993;680-692.
    • (1993) J. Mol. Biol. , vol.232 , pp. 680-692
    • Montgomery, D.1    Jordan, R.2    McMacken, R.3    Freire, E.4
  • 33
    • 0029038683 scopus 로고
    • The peptide-binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology
    • Morshauser R. C., Wang H., Flynn G. C., Zuiderweg E. R. P. The peptide-binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology. Biochemistry. 34:1995;6261-6266.
    • (1995) Biochemistry , vol.34 , pp. 6261-6266
    • Morshauser, R.C.1    Wang, H.2    Flynn, G.C.3    Zuiderweg, E.R.P.4
  • 34
    • 0028125904 scopus 로고
    • How frequent are correlated changes in families of protein sequences?
    • Neher E. How frequent are correlated changes in families of protein sequences? Proc. Natl Acad. Sci. USA, 91:1994;98-102.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 98-102
    • Neher, E.1
  • 35
    • 0001441922 scopus 로고    scopus 로고
    • Calculation of symmetric multimer structures from NMR data using a priori knowledge of the monomer structure, co-monomer restraints, and interface mapping: The case of leucine zippers
    • O'Donoghue S., King G., Nilges M. Calculation of symmetric multimer structures from NMR data using a priori knowledge of the monomer structure, co-monomer restraints, and interface mapping: the case of leucine zippers. J. Biomol. NMR, 8:1996;193-206.
    • (1996) J. Biomol. NMR , vol.8 , pp. 193-206
    • O'Donoghue, S.1    King, G.2    Nilges, M.3
  • 36
    • 0030927252 scopus 로고    scopus 로고
    • A graphical interface for correlated mutations and other structure prediction methods
    • Pazos F., Olmea O., Valencia A. A graphical interface for correlated mutations and other structure prediction methods. CABIOS. 13:1997;319-321.
    • (1997) CABIOS , vol.13 , pp. 319-321
    • Pazos, F.1    Olmea, O.2    Valencia, A.3
  • 37
    • 0018168011 scopus 로고
    • Hemoglobin structure and respiratory transport
    • Perutz M. F. Hemoglobin structure and respiratory transport. Sci. Am. 239(6):1978;92-125.
    • (1978) Sci. Am. , vol.2396 , pp. 92-125
    • Perutz, M.F.1
  • 39
    • 0027288463 scopus 로고
    • The HSSP data base of protein structure-sequence alignments
    • Sander C., Schneider R. The HSSP data base of protein structure-sequence alignments. Nucl. Acids Res. 21:1993;3105-3109.
    • (1993) Nucl. Acids Res. , vol.21 , pp. 3105-3109
    • Sander, C.1    Schneider, R.2
  • 40
    • 0025093185 scopus 로고
    • Estimating the contribution of engineered surface electrostatic interactions to protein stability using double mutant cycles
    • Serrano L., Horovitz A., Avron B., Bycroft M., Fersht A. R. Estimating the contribution of engineered surface electrostatic interactions to protein stability using double mutant cycles. Biochemistry. 29:1990;9343-9352.
    • (1990) Biochemistry , vol.29 , pp. 9343-9352
    • Serrano, L.1    Horovitz, A.2    Avron, B.3    Bycroft, M.4    Fersht, A.R.5
  • 41
    • 0028084754 scopus 로고
    • Can three-dimensional contacts in protein structures be predicted by analysis of correlated mutations
    • Shindyalov I. N., Kolchanov N. A., Sander C. Can three-dimensional contacts in protein structures be predicted by analysis of correlated mutations. Protein Eng. 7:1994;349-358.
    • (1994) Protein Eng. , vol.7 , pp. 349-358
    • Shindyalov, I.N.1    Kolchanov, N.A.2    Sander, C.3
  • 42
    • 0025785057 scopus 로고
    • Protein docking and complementarity
    • Shoichet B. K., Kuntz J. I. D. Protein docking and complementarity. Mol. Biol. 221:1991;327-346.
    • (1991) Mol. Biol. , vol.221 , pp. 327-346
    • Shoichet, B.K.1    Kuntz, J.I.D.2
  • 43
    • 0028943588 scopus 로고
    • Continuous and discontinuous domains: An algorithm for the automatic generation of reliable protein domain definitions
    • Siddiqui A., Barton J. Continuous and discontinuous domains: an algorithm for the automatic generation of reliable protein domain definitions. Protein Sci. 4:1995;872-884.
    • (1995) Protein Sci. , vol.4 , pp. 872-884
    • Siddiqui, A.1    Barton, J.2
  • 44
    • 0028914725 scopus 로고
    • An automatic method involving cluster analysis of secondary structures for the identification of domains in proteins
    • Sowdhamini R., Blundell T. An automatic method involving cluster analysis of secondary structures for the identification of domains in proteins. Protein Sci. 4:1994;506-520.
    • (1994) Protein Sci. , vol.4 , pp. 506-520
    • Sowdhamini, R.1    Blundell, T.2
  • 45
    • 0026700029 scopus 로고
    • Prediction of the structure of a receptor-protein complex usong a binary docking method
    • Stoddard B. L., Koshland D. E. Prediction of the structure of a receptor-protein complex usong a binary docking method. Nature. 358:1992;774-776.
    • (1992) Nature , vol.358 , pp. 774-776
    • Stoddard, B.L.1    Koshland, D.E.2
  • 47
    • 0028937153 scopus 로고
    • A procedure for detecting structural domains in proteins
    • Swindells M. B. A procedure for detecting structural domains in proteins. Protein Sci. 4:1994;103-112.
    • (1994) Protein Sci. , vol.4 , pp. 103-112
    • Swindells, M.B.1
  • 48
    • 0027952860 scopus 로고
    • Compensating changes in protein multiple sequence alignments
    • Taylor W. R., Hatrick K. Compensating changes in protein multiple sequence alignments. Protein Eng. 7:1994;341-348.
    • (1994) Protein Eng. , vol.7 , pp. 341-348
    • Taylor, W.R.1    Hatrick, K.2
  • 49
    • 0028410583 scopus 로고
    • Detailed ab initio prediction of lysozyme-antibody complex with 1.6 Å accuracy
    • Totrov M. M., Abagyan R. A. Detailed ab initio prediction of lysozyme-antibody complex with 1.6 Å accuracy. Nature Struct. Biol. 1:1994;259-263.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 259-263
    • Totrov, M.M.1    Abagyan, R.A.2
  • 50
    • 0029988383 scopus 로고    scopus 로고
    • Protein-protein interfaces: Architectures and interactions in protein-protein interfaces and in protein cores. Their similarities and differences
    • Tsai C. J., Lin S. L., Wolfson H. J., Nussinov R. Protein-protein interfaces: architectures and interactions in protein-protein interfaces and in protein cores. Their similarities and differences. Crit. Rev. Biochem. Mol. Biol. 31:1996;127-152.
    • (1996) Crit. Rev. Biochem. Mol. Biol. , vol.31 , pp. 127-152
    • Tsai, C.J.1    Lin, S.L.2    Wolfson, H.J.3    Nussinov, R.4
  • 51
    • 0026560853 scopus 로고
    • Correlation of co-ordinated amino acid changes at the two-domain interface of cysteine proteases with protein stability
    • Vernet T., Tessier D. C., Khouri H. E. Correlation of co-ordinated amino acid changes at the two-domain interface of cysteine proteases with protein stability. J. Mol. Biol. 224:1992;501-509.
    • (1992) J. Mol. Biol. , vol.224 , pp. 501-509
    • Vernet, T.1    Tessier, D.C.2    Khouri, H.E.3
  • 52
    • 0026464639 scopus 로고
    • New algorithm to model protein-protein recognition based on surface complementarity. Applications to antibody-antigen docking
    • Walls P. H., Sternberg M. J. New algorithm to model protein-protein recognition based on surface complementarity. Applications to antibody-antigen docking. J. Mol. Biol. 228:1992;277-297.
    • (1992) J. Mol. Biol. , vol.228 , pp. 277-297
    • Walls, P.H.1    Sternberg, M.J.2
  • 53
    • 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


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