메뉴 건너뛰기




Volumn 78, Issue 6, 2010, Pages 1563-1574

Amino acid substitutions at protein-protein interfaces that modulate the oligomeris state

Author keywords

Hotspot; Protein complexes; Protein family; Protein protein interactions; Shadow interfaces

Indexed keywords

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; DISSOCIATION; HYDROPHOBICITY; OLIGOMERIZATION; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE;

EID: 77951243441     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22673     Document Type: Article
Times cited : (12)

References (51)
  • 6
    • 33644550021 scopus 로고    scopus 로고
    • Structural systems biology: Modelling protein interactions
    • DOI 10.1038/nrm1859, PII N1859
    • Aloy P, Russell RB. Structural systems biology: modelling protein interactions. Nat Rev Mol Cell Biol 2006;7:188-197. (Pubitemid 43297948)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.3 , pp. 188-197
    • Aloy, P.1    Russell, R.B.2
  • 7
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones S, Thornton JM. Principles of protein-protein interactions. Proc Natl Acad Sci USA 1996;93:13-20.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 8
    • 0041312697 scopus 로고    scopus 로고
    • Diversity of protein-protein interactions
    • Nooren IM, Thornton JM. Diversity of protein-protein interactions. EMBO J 2003;22:3486-3492.
    • (2003) EMBO J , vol.22 , pp. 3486-3492
    • Nooren, I.M.1    Thornton, J.M.2
  • 9
    • 0031565729 scopus 로고    scopus 로고
    • Analysis of protein-protein interaction sites using surface patches
    • DOI 10.1006/jmbi.1997.1234
    • Jones S, Thornton JM. Analysis of protein-protein interaction sites using surface patches. J Mol Biol 1997;272:121-132. (Pubitemid 27395542)
    • (1997) Journal of Molecular Biology , vol.272 , Issue.1 , pp. 121-132
    • Jones, S.1    Thornton, J.M.2
  • 10
    • 0028607523 scopus 로고
    • Cavities and packing at protein interfaces
    • Hubbard SJ, Argos P. Cavities and packing at protein interfaces. Protein Sc 1994;3:2194-2206.
    • (1994) Protein Sc , vol.3 , pp. 2194-2206
    • Hubbard, S.J.1    Argos, P.2
  • 11
    • 0031547966 scopus 로고    scopus 로고
    • Electrostatic complementarity at protein/protein interfaces
    • McCoy AJ, Chandana Epa V, Colman PM. Electrostatic complementarity at protein/protein interfaces. J Mol Biol 1997;268:570-584.
    • (1997) J Mol Biol , vol.268 , pp. 570-584
    • McCoy, A.J.1    Chandana Epa, V.2    Colman, P.M.3
  • 12
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • DOI 10.1006/jmbi.1998.2439
    • Lo Conte L, Chothia C, Janin J. The atomic structure of proteinprotein recognition sites. J Mol Biol 1999;285:2177-2198. (Pubitemid 29078179)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.5 , pp. 2177-2198
    • Conte, L.L.1    Chothia, C.2    Janin, J.3
  • 13
  • 14
    • 0035342450 scopus 로고    scopus 로고
    • Residue frequencies and pairing preferences at protein-protein interfaces
    • Glaser F, Steinberg DM, Vakser IA, Ben-Tal N. Residue frequencies and pairing preferences at protein-protein interfaces. Proteins 2001;43:89-102.
    • (2001) Proteins , vol.43 , pp. 89-102
    • Glaser, F.1    Steinberg, D.M.2    Vakser, I.A.3    Ben-Tal, N.4
  • 15
    • 1042275583 scopus 로고    scopus 로고
    • A Dissection of Specific and Non-specific Protein-Protein Interfaces
    • DOI 10.1016/j.jmb.2003.12.073
    • Bahadur RP, Chakrabarti P, Rodier F, Janin J. A dissection of specific and non-specific protein-protein interfaces. J Mol Biol 2004; 336:943-955. (Pubitemid 38201541)
    • (2004) Journal of Molecular Biology , vol.336 , Issue.4 , pp. 943-955
    • Bahadur, R.P.1    Chakrabarti, P.2    Rodier, F.3    Janin, J.4
  • 16
    • 0037474541 scopus 로고    scopus 로고
    • Structural characterisation and functional significance of transient protein-protein interactions
    • Nooren IM, Thornton JM. Structural characterisation and functional significance of transient protein-protein interactions. J Mol Biol 2003;325:991-1018.
    • (2003) J Mol Biol , vol.325 , pp. 991-1018
    • Nooren, I.M.1    Thornton, J.M.2
  • 17
    • 0037229456 scopus 로고    scopus 로고
    • Analysing six types of protein-protein interfaces
    • DOI 10.1016/S0022-2836(02)01223-8
    • Ofran Y, Rost B. Analysing six types of protein-protein interfaces. J Mol Biol 2003;325:377-387. (Pubitemid 36062695)
    • (2003) Journal of Molecular Biology , vol.325 , Issue.2 , pp. 377-387
    • Ofran, Y.1    Rost, B.2
  • 19
    • 32344445231 scopus 로고    scopus 로고
    • NMR studies of protein interactions
    • Takeuchi K, Wagner G. NMR studies of protein interactions. Curr Opin Struct Biol 2006;16:109-117.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 109-117
    • Takeuchi, K.1    Wagner, G.2
  • 21
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan AA, Thorn KS. Anatomy of hot spots in protein interfaces. J Mol Biol 1998;280:1-9.
    • (1998) J Mol Biol , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 22
    • 34548779127 scopus 로고    scopus 로고
    • Hot spots-a review of the protein-protein interface determinant amino-acid residues
    • Moreira IS, Fernandes PA, Ramos MJ. Hot spots-a review of the protein-protein interface determinant amino-acid residues. Proteins 2007;68:803-812.
    • (2007) Proteins , vol.68 , pp. 803-812
    • Moreira, I.S.1    Fernandes, P.A.2    Ramos, M.J.3
  • 24
    • 7944225979 scopus 로고    scopus 로고
    • Protein-protein interactions: Hot spots and structurally conserved residues often locate in complemented pockets that pre-organized in the unbound states: Implications for docking
    • DOI 10.1016/j.jmb.2004.09.051, PII S0022283604012070
    • Li X, Keskin O, Ma B, Nussinov R, Liang J. Protein-protein interactions: hot spots and structurally conserved residues often locate in complemented pockets that pre-organized in the unbound states: implications for docking. J Mol Biol 2004;344:781-795. (Pubitemid 39469220)
    • (2004) Journal of Molecular Biology , vol.344 , Issue.3 , pp. 781-795
    • Li, X.1    Keskin, O.2    Ma, B.3    Nussinov, R.4    Liang, J.5
  • 25
    • 22244465254 scopus 로고    scopus 로고
    • Protein-protein interactions: Organization, cooperativity and mapping in a bottom-up Systems Biology approach
    • DOI 10.1088/1478-3975/2/2/S03
    • Keskin O, Ma B, Rogale K, Gunasekaran K, Nussinov R. Proteinprotein interactions: organization, cooperativity and mapping in a bottom-up Systems Biology approach. Phys Biol 2005;2:S24-S35. (Pubitemid 40991705)
    • (2005) Physical Biology , vol.2 , Issue.2
    • Keskin, O.1    Ma, B.2    Rogale, K.3    Gunasekaran, K.4    Nussinov, R.5
  • 26
    • 0035178383 scopus 로고    scopus 로고
    • Protein-protein interfaces: Analysis of amino acid conservation in homodimers
    • Valdar WS, Thornton JM. Protein-protein interfaces: analysis of amino acid conservation in homodimers. Proteins 2001;42:108-124.
    • (2001) Proteins , vol.42 , pp. 108-124
    • Valdar, W.S.1    Thornton, J.M.2
  • 27
    • 0346733329 scopus 로고    scopus 로고
    • Are protein-protein interfaces more conserved in sequence than the rest of the protein surface?
    • Caffrey DR, Somaroo S, Hughes JD, Mintseris J, Huang ES. Are protein-protein interfaces more conserved in sequence than the rest of the protein surface? Protein Sci 2004;13:190-202.
    • (2004) Protein Sci , vol.13 , pp. 190-202
    • Caffrey, D.R.1    Somaroo, S.2    Hughes, J.D.3    Mintseris, J.4    Huang, E.S.5
  • 30
    • 34547573955 scopus 로고    scopus 로고
    • Protein-protein interaction hotspots carved into sequences
    • DOI 10.1371/journal.pcbi.0030119
    • Ofran Y, Rost B. Protein-protein interaction hotspots carved into sequences. PLoS Comput Biol. 2007;3:e119. (Pubitemid 47196162)
    • (2007) PLoS Computational Biology , vol.3 , Issue.7 , pp. 1169-1176
    • Ofran, Y.1    Rost, B.2
  • 31
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin AG, Brenner SE, Hubbard T, 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.3    Chothia, C.4
  • 32
    • 0035943382 scopus 로고    scopus 로고
    • Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 Å resolution
    • DOI 10.1006/jmbi.2001.4853
    • Dedercq JP, Evrard C, Clippe A, Stricht DV, Bernard A, Knoops B. Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 A resolution. J Mol Biol 2001;311:751-759. (Pubitemid 32803733)
    • (2001) Journal of Molecular Biology , vol.311 , Issue.4 , pp. 751-759
    • Declercq, J.-P.1    Evrard, C.2    Clippe, A.3    Stricht, D.V.4    Bernard, A.5    Knoops, B.6
  • 34
    • 0036081012 scopus 로고    scopus 로고
    • BRENDA, enzyme data and metabolic information
    • Schomburg I, Chang A, Schomburg D. BRENDA, enzyme data and metabolic information. Nucleic Acids Res 2002;30:47-49. (Pubitemid 34679500)
    • (2002) Nucleic Acids Research , vol.30 , Issue.1 , pp. 47-49
    • Schomburg, I.1    Chang, A.2    Schomburg, D.3
  • 35
    • 35748959334 scopus 로고    scopus 로고
    • PiQSi; protein quaternary structure investigation
    • Levy ED. PiQSi; protein quaternary structure investigation, Structure 2007;15:1364-1367.
    • (2007) Structure , vol.15 , pp. 1364-1367
    • Levy, E.D.1
  • 36
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • DOI 10.1016/j.jmb.2007.05.022, PII S0022283607006420
    • Krissinel E, Henrick K. Inference of macromolecular assemblies from crystalline state. J Mol Biol 2007;372:774-797. (Pubitemid 47321791)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 37
    • 0032169688 scopus 로고    scopus 로고
    • PQS: A protein quaternary structure file server
    • DOI 10.1016/S0968-0004(98)01253-5, PII S0968000498012535
    • Henrick K, Thornton J. PQS: a protein quaternary structure file server. Trends Biochem Sci 1998;23:358-361. (Pubitemid 28461869)
    • (1998) Trends in Biochemical Sciences , vol.23 , Issue.9 , pp. 358-361
    • Henrick, K.1    Thornton, J.M.2
  • 40
    • 0022412192 scopus 로고
    • Hydrophobicity of amino acid residues in globular proteins
    • Rose GD, Geselowitz AR, Lesser GJ, Lee RH, Zehfus MH. Hydrophobicity of amino acid residues in globular proteins. Science 1985; 229:834-838. (Pubitemid 16246583)
    • (1985) Science , vol.229 , Issue.4716 , pp. 834-838
    • Rose, G.D.1    Geselowitz, A.R.2    Lesser, G.J.3
  • 41
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopoiymers 1983;22:2577-2637.
    • (1983) Biopoiymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 42
    • 0041620359 scopus 로고    scopus 로고
    • MATRAS: A program for protein 3D structure comparison
    • DOI 10.1093/nar/gkg581
    • Kawabata T. MATRAS: A program for protein 3D structure comparison. Nucleic Acids Res 2003;31:3367-3369. (Pubitemid 37442161)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3367-3369
    • Kawabata, T.1
  • 43
    • 0026636312 scopus 로고
    • Hydrophobicity and structural classes in proteins
    • Cid H, Bunster M, Canales M, Gazitua F. Hydrophobicity and structural classes in proteins. Protein Eng 1992;5:373-375.
    • (1992) Protein Eng , vol.5 , pp. 373-375
    • Cid, H.1    Bunster, M.2    Canales, M.3    Gazitua, F.4
  • 44
  • 45
    • 0001884644 scopus 로고
    • Individual comparisons by ranking methods
    • Wilcoxon F. Individual Comparisons by Ranking Methods. Biometrics Bull 1945;1:80-83.
    • (1945) Biometrics Bull , vol.1 , pp. 80-83
    • Wilcoxon, F.1
  • 47
    • 77951209467 scopus 로고    scopus 로고
    • MolFeat. Version 3.0. Tokyo: FiatLux Corporation: 2006
    • MolFeat. Version 3.0. Tokyo: FiatLux Corporation: 2006.
  • 48
    • 0033561427 scopus 로고    scopus 로고
    • Crystal structures of Bacillus caldovelox arginase in complex with substrate and inhibitors reveal new insights into activation, inhibition and catalysis in the arginase superfamily
    • Bewley MC, Jeffrey PD, Patchett ML, Kanyo ZF, Baker EN. Crystal structures of Bacillus caldovelox arginase in complex with substrate and inhibitors reveal new insights into activation, inhibition and catalysis in the arginase superfamily. Structure 1999;7: 435-448.
    • (1999) Structure , vol.7 , pp. 435-448
    • Bewley, M.C.1    Jeffrey, P.D.2    Patchett, M.L.3    Kanyo, Z.F.4    Baker, E.N.5
  • 49
    • 0034737320 scopus 로고    scopus 로고
    • The crystal structure of dihydrofolate reductase from Thermotoga maritima: Molecular features of thermostability
    • Dams T, Auerbach G, Bader G, Jacob U, Ploom T, Huber R, Jaenicke R. The crystal structure of dihydrofolate reductase from Thermotoga maritima: molecular features of thermostability. J Mol Biol 2000;297:659-672.
    • (2000) J Mol Biol , vol.297 , pp. 659-672
    • Dams, T.1    Auerbach, G.2    Bader, G.3    Jacob, U.4    Ploom, T.5    Huber, R.6    Jaenicke, R.7
  • 51
    • 51649094321 scopus 로고    scopus 로고
    • Built-in loops allow versatility in domain-domain interactions: Lessons from self-interacting domains
    • Akiva E, Itzhaki Z, Margalit H. Built-in loops allow versatility in domain-domain interactions: lessons from self-interacting domains. Proc Natl Acad Sci USA 2008;105:13292-13297.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 13292-13297
    • Akiva, E.1    Itzhaki, Z.2    Margalit, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.