메뉴 건너뛰기




Volumn 29, Issue , 2000, Pages 105-153

Structural symmetry and protein function

Author keywords

Oligomeric proteins; Protein structure function relationships; Protein symmetry

Indexed keywords

COMPLEX FORMATION; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN STRUCTURE; REVIEW; STRUCTURE ACTIVITY RELATION;

EID: 0033886522     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.biophys.29.1.105     Document Type: Review
Times cited : (783)

References (101)
  • 1
    • 0028114231 scopus 로고
    • Structure at 2.8 angstroms resolution of F1-ATPase from bovine heart mitochondria
    • 1. Abrahams JP, Leslie AGW, Lutter R, Walker JE. 1994. Structure at 2.8 angstroms resolution of F1-ATPase from bovine heart mitochondria. Nature 370:621-28
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.W.2    Lutter, R.3    Walker, J.E.4
  • 3
    • 0024322304 scopus 로고
    • The allosteric transition of glycogen phosphorylase
    • 3. Barford D, Johnson LN. 1989. The allosteric transition of glycogen phosphorylase. Nature 340:609-16
    • (1989) Nature , vol.340 , pp. 609-616
    • Barford, D.1    Johnson, L.N.2
  • 4
    • 0028865843 scopus 로고
    • 3D domain swapping: A mechanism for oligomer assembly
    • 4. Bennett MJ, Schlunegger MP, Eisenberg D. 1995. 3D domain swapping: a mechanism for oligomer assembly. Protein Sci. 4:2455-68
    • (1995) Protein Sci. , vol.4 , pp. 2455-2468
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 5
    • 0031928582 scopus 로고    scopus 로고
    • On the structure of the scaffolding core of bacteriophage T4 and its role in head length determination
    • 5. Berger B, Shor PW. 1998. On the structure of the scaffolding core of bacteriophage T4 and its role in head length determination. J. Struct. Biol. 121:285-94
    • (1998) J. Struct. Biol. , vol.121 , pp. 285-294
    • Berger, B.1    Shor, P.W.2
  • 6
    • 0032215219 scopus 로고    scopus 로고
    • At sixes and sevens: Characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease
    • 6. Beuron F, Maurizi MR, Belnap DM, Kocsis E, Booy FP, et al. 1998. At sixes and sevens: characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease. J. Struct. Biol. 123:248-59
    • (1998) J. Struct. Biol. , vol.123 , pp. 248-259
    • Beuron, F.1    Maurizi, M.R.2    Belnap, D.M.3    Kocsis, E.4    Booy, F.P.5
  • 7
    • 77956751025 scopus 로고
    • Insulin: The structure in the crystal and its reflection in chemistry and biology
    • 7. Blundell T, Dodson G, Hodgkin D, Mercola D. 1972. Insulin: the structure in the crystal and its reflection in chemistry and biology. Adv. Protein Chem. 26:279-402
    • (1972) Adv. Protein Chem. , vol.26 , pp. 279-402
    • Blundell, T.1    Dodson, G.2    Hodgkin, D.3    Mercola, D.4
  • 8
    • 0029949156 scopus 로고    scopus 로고
    • Symmetry, stability, and dynamics of multidomain and multicomponent protein systems
    • 8. Blundell TL, Srinivasan N. 1996. Symmetry, stability, and dynamics of multidomain and multicomponent protein systems. Proc. Natl. Acad. Sci. USA 93:14243-48
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14243-14248
    • Blundell, T.L.1    Srinivasan, N.2
  • 9
    • 0027492268 scopus 로고
    • The binding site change mechanism for ATP synthase - Some probabilities and possibilities
    • 9. Boyer PD. 1993. The binding site change mechanism for ATP synthase - some probabilities and possibilities. Biochim. Biophys. Acta 1140:215-50
    • (1993) Biochim. Biophys. Acta , vol.1140 , pp. 215-250
    • Boyer, P.D.1
  • 10
    • 0017841508 scopus 로고
    • Change of waveform in bacterial flagella: The role of mechanics at the molecular level
    • 10. Calladine CR. 1978. Change of waveform in bacterial flagella: the role of mechanics at the molecular level. J. Mol. Biol. 118:457-79
    • (1978) J. Mol. Biol. , vol.118 , pp. 457-479
    • Calladine, C.R.1
  • 13
    • 0026289204 scopus 로고
    • Asymmetry in protein structures
    • 13. Chothia C. 1991. Asymmetry in protein structures. CIBA Found. Symp. 162:36-57
    • (1991) CIBA Found. Symp. , vol.162 , pp. 36-57
    • Chothia, C.1
  • 14
    • 0016708122 scopus 로고
    • Principles of protein-protein recognition
    • 14. Chothia C, Janin J. 1975. Principles of protein-protein recognition. Nature 256: 705-8
    • (1975) Nature , vol.256 , pp. 705-708
    • Chothia, C.1    Janin, J.2
  • 15
    • 0021381587 scopus 로고
    • Properties and metabolism of the aqueous cytoplasm and its boundaries
    • 15. Clegg JS. 1984. Properties and metabolism of the aqueous cytoplasm and its boundaries. Am. J. Physiol. 246:R133-51
    • (1984) Am. J. Physiol. , vol.246
    • Clegg, J.S.1
  • 16
    • 0015239530 scopus 로고
    • The quaternary structure of proteins composed of identical subunits
    • 16. Cornish-Bowden AJ, Koshland DE Jr. 1971. The quaternary structure of proteins composed of identical subunits. J. Biol. Chem. 246:3092-102
    • (1971) J. Biol. Chem. , vol.246 , pp. 3092-3102
    • Cornish-Bowden, A.J.1    Koshland D.E., Jr.2
  • 17
    • 0001423375 scopus 로고
    • Principles and problems of biological growth
    • June
    • 17. Crane HR. 1950. Principles and problems of biological growth. Sci. Monthly June:376-89
    • (1950) Sci. Monthly , pp. 376-389
    • Crane, H.R.1
  • 18
    • 36949077319 scopus 로고
    • Structure of small viruses
    • 18. Crick FHC, Watson JD. 1956. Structure of small viruses. Nature 177:473-75
    • (1956) Nature , vol.177 , pp. 473-475
    • Crick, F.H.C.1    Watson, J.D.2
  • 20
    • 0015313012 scopus 로고
    • The influence of polyvalency on the binding properties of antibodies
    • 20. Crothers DM, Metzger H. 1972. The influence of polyvalency on the binding properties of antibodies. Immunochemistry 9:341-57
    • (1972) Immunochemistry , vol.9 , pp. 341-357
    • Crothers, D.M.1    Metzger, H.2
  • 21
    • 0001497377 scopus 로고
    • Enzymes with asymmetrically arranged subunits
    • 21. Degani Y, Degani C. 1980. Enzymes with asymmetrically arranged subunits. Trends Biochem. Sci. 5:337-41
    • (1980) Trends Biochem. Sci. , vol.5 , pp. 337-341
    • Degani, Y.1    Degani, C.2
  • 22
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • 22. DeVos AM, Ultsch M, Kossiakoff AA. 1992. Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science 255:306-12
    • (1992) Science , vol.255 , pp. 306-312
    • DeVos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 23
    • 0000814652 scopus 로고
    • Structural aspects of allostery
    • 23. Evans PR. 1991. Structural aspects of allostery. Curr. Opin. Struct. Biol. 1:773-79
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 773-779
    • Evans, P.R.1
  • 24
    • 0020184671 scopus 로고
    • How crowded is the cytoplasm?
    • 24. Fulton AB. 1982. How crowded is the cytoplasm? Cell 30:345-47
    • (1982) Cell , vol.30 , pp. 345-347
    • Fulton, A.B.1
  • 26
    • 0029856117 scopus 로고    scopus 로고
    • Symmetries throughout organic evolution
    • 26. Garcia-Bellido A. 1996. Symmetries throughout organic evolution. Proc. Natl. Acad. Sci. USA 93:14229-32
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14229-14232
    • Garcia-Bellido, A.1
  • 28
    • 0027499733 scopus 로고
    • Soluble proteins: Size, shape and function
    • 28. Goodsell DS, Olson AJ. 1993. Soluble proteins: size, shape and function. Trends Biochem. Sci. 18:65-68
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 65-68
    • Goodsell, D.S.1    Olson, A.J.2
  • 29
    • 0025016827 scopus 로고
    • Crystal structures of phosphoacetamide ligated T and phosphoacetamide and malonate ligated R states of aspartate carbamoyltransferase at 2.8-Å resolution and neutral pH
    • 29. Gouax JE, Lipscomb WN. 1990. Crystal structures of phosphoacetamide ligated T and phosphoacetamide and malonate ligated R states of aspartate carbamoyltransferase at 2.8-Å resolution and neutral pH. Biochemistry 29:389-402
    • (1990) Biochemistry , vol.29 , pp. 389-402
    • Gouax, J.E.1    Lipscomb, W.N.2
  • 30
    • 0000439629 scopus 로고
    • The reaction with red cells of 7S rabbit antibody, its sub-units and their recombinants
    • 30. Greenbury CL, Moore DH, Nunn LAC. 1965. The reaction with red cells of 7S rabbit antibody, its sub-units and their recombinants. Immunology 8:420-31
    • (1965) Immunology , vol.8 , pp. 420-431
    • Greenbury, C.L.1    Moore, D.H.2    Nunn, L.A.C.3
  • 32
    • 0030897031 scopus 로고    scopus 로고
    • Structure of the 20s proteasome from yeast at 2.4 Å resolution
    • 32. Groll M, Ditzel L, Lowe J, Stock D, Bochtler M, et al. 1997. Structure of the 20S proteasome from yeast at 2.4 Å resolution. Nature 386:463-71
    • (1997) Nature , vol.386 , pp. 463-471
    • Groll, M.1    Ditzel, L.2    Lowe, J.3    Stock, D.4    Bochtler, M.5
  • 33
    • 0014030843 scopus 로고
    • Symmetry of protein oligomers formed by isologous association
    • 33. Hanson KR. 1966. Symmetry of protein oligomers formed by isologous association. J. Mol. Biol. 22:405-9
    • (1966) J. Mol. Biol. , vol.22 , pp. 405-409
    • Hanson, K.R.1
  • 36
    • 0039538633 scopus 로고
    • Symmetry mismatch and DNA packaging in large bacteriophages
    • 36. Hendrix RW. 1978. Symmetry mismatch and DNA packaging in large bacteriophages. Proc. Natl. Acad. Sci. USA 75:4779-83
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4779-4783
    • Hendrix, R.W.1
  • 37
    • 0030034288 scopus 로고    scopus 로고
    • DNA polymerase III: Running rings around the fork
    • 37. Herendeen DR, Kelly TJ. 1996. DNA polymerase III: running rings around the fork. Cell 84:5-8
    • (1996) Cell , vol.84 , pp. 5-8
    • Herendeen, D.R.1    Kelly, T.J.2
  • 38
  • 39
    • 0017342711 scopus 로고
    • On the influence of polyvalent ligands on membrane curvature
    • 39. Hewitt JA. 1977. On the influence of polyvalent ligands on membrane curvature. J. Theor. Biol. 64:455-72
    • (1977) J. Theor. Biol. , vol.64 , pp. 455-472
    • Hewitt, J.A.1
  • 40
    • 67649893105 scopus 로고
    • Physical cluster mechanics: Statistical thermodynamics and nucleation theory for monatomic systems
    • 40. Hoare MR, Pal P. 1975. Physical cluster mechanics: statistical thermodynamics and nucleation theory for monatomic systems. Adv. Phys. 24:645-78
    • (1975) Adv. Phys. , vol.24 , pp. 645-678
    • Hoare, M.R.1    Pal, P.2
  • 41
    • 0028403259 scopus 로고
    • T and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric control
    • 41. Iwata S, Kamata K, Yoshida S, Minowa T, Ohta T. 1994. T and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric control. Nature Struct. Biol. 1:176-85
    • (1994) Nature Struct. Biol. , vol.1 , pp. 176-185
    • Iwata, S.1    Kamata, K.2    Yoshida, S.3    Minowa, T.4    Ohta, T.5
  • 42
    • 0031588020 scopus 로고    scopus 로고
    • Quasiequivalent viruses: A paradigm for protein assemblies
    • 42. Johnson JE, Speir JA. 1997. Quasiequivalent viruses: a paradigm for protein assemblies. J. Mol. Biol. 269:665-75
    • (1997) J. Mol. Biol. , vol.269 , pp. 665-675
    • Johnson, J.E.1    Speir, J.A.2
  • 45
    • 0018791734 scopus 로고
    • Transition of bacterial flagella from helical to straight forms with different subunit arrangements
    • 45. Kamiya R, Asakura S, Wakabayashi K, Namba K. 1979. Transition of bacterial flagella from helical to straight forms with different subunit arrangements. J. Mol. Biol. 131:725-42
    • (1979) J. Mol. Biol. , vol.131 , pp. 725-742
    • Kamiya, R.1    Asakura, S.2    Wakabayashi, K.3    Namba, K.4
  • 46
    • 0025297775 scopus 로고
    • Form determination of the heads of bacteriophages
    • 46. Kellenberger E. 1990. Form determination of the heads of bacteriophages. Eur. J. Biochem. 190:233-48
    • (1990) Eur. J. Biochem. , vol.190 , pp. 233-248
    • Kellenberger, E.1
  • 48
    • 0014197637 scopus 로고
    • Protein subunits: A table
    • 48. Klotz IM. 1967. Protein subunits: a table. Science 155:697-98
    • (1967) Science , vol.155 , pp. 697-698
    • Klotz, I.M.1
  • 52
    • 0026693137 scopus 로고
    • Crystal structure at 3.5 Å resolution of HIV-1 reverse transcriptase complexed with an inhibitor
    • 52. Kohlstaedt LA, Wang J, Friedman JM, Rice PA, Steitz TA. 1992. Crystal structure at 3.5 Å resolution of HIV-1 reverse transcriptase complexed with an inhibitor. Science 256:1783-89
    • (1992) Science , vol.256 , pp. 1783-1789
    • Kohlstaedt, L.A.1    Wang, J.2    Friedman, J.M.3    Rice, P.A.4    Steitz, T.A.5
  • 53
    • 0026717535 scopus 로고
    • Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: A sliding DNA clamp
    • 53. Kong X-P, Onrust R, O-Donnell M, Kuriyan J. 1992. Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp. Cell 69:425-37
    • (1992) Cell , vol.69 , pp. 425-437
    • Kong, X.-P.1    Onrust, R.2    O-Donnell, M.3    Kuriyan, J.4
  • 54
    • 0016988002 scopus 로고
    • The evolution of function in enzymes
    • 54. Koshland DE. 1976. The evolution of function in enzymes. Fed. Proc. 35:2104-11
    • (1976) Fed. Proc. , vol.35 , pp. 2104-2111
    • Koshland, D.E.1
  • 55
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • 55. Koshland DE, Nemethy G, Filmer D. 1966. Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 5:365-85
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland, D.E.1    Nemethy, G.2    Filmer, D.3
  • 56
    • 0028618183 scopus 로고
    • Crystal structure of the eukaryotic DNA processivity factor PCNA
    • 56. Krishna TSR, Kong X-P, Gary S, Burgers PM, Kuriyan J. 1994. Crystal structure of the eukaryotic DNA processivity factor PCNA. Cell 79:1233-43
    • (1994) Cell , vol.79 , pp. 1233-1243
    • Krishna, T.S.R.1    Kong, X.-P.2    Gary, S.3    Burgers, P.M.4    Kuriyan, J.5
  • 57
    • 0027104840 scopus 로고
    • Translational accuracy and the fitness of bacteria
    • 57. Kurland CG. 1992. Translational accuracy and the fitness of bacteria. Annu. Rev. Genet. 26:29-50
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 29-50
    • Kurland, C.G.1
  • 58
    • 0028824480 scopus 로고
    • Titins: Giant proteins in charge of muscle ultrastructure and elasticity
    • 58. Labeit S, Kolmerer B. 1995. Titins: giant proteins in charge of muscle ultrastructure and elasticity. Science 270:293-96
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 59
    • 0024293363 scopus 로고
    • Heavy riboflavin synthase from Bacillus subtilis: Crystal structure analysis of the icosahedral beta-60 capsid at 3.3 a resolution
    • 59. Ladenstein R, Schneider M, Huber R, Bartunik H-D, Wilson K, et al. 1988. Heavy riboflavin synthase from Bacillus subtilis: crystal structure analysis of the icosahedral beta-60 capsid at 3.3 A resolution. J. Mol. Biol. 203:1045-70
    • (1988) J. Mol. Biol. , vol.203 , pp. 1045-1070
    • Ladenstein, R.1    Schneider, M.2    Huber, R.3    Bartunik, H.-D.4    Wilson, K.5
  • 60
    • 0032522670 scopus 로고    scopus 로고
    • Morphology of protein-protein interfaces
    • 60. Larsen TA, Olson AJ, Goodsell DS. 1998. Morphology of protein-protein interfaces. Structure 6:421-27
    • (1998) Structure , vol.6 , pp. 421-427
    • Larsen, T.A.1    Olson, A.J.2    Goodsell, D.S.3
  • 61
    • 0023010495 scopus 로고
    • Ricin subunit association: Thermodynamics and the role of the disulfide bond in toxicity
    • 61. Lewis MS, Youle RJ. 1986. Ricin subunit association: thermodynamics and the role of the disulfide bond in toxicity. J. Biol. Chem. 261:11571-77
    • (1986) J. Biol. Chem. , vol.261 , pp. 11571-11577
    • Lewis, M.S.1    Youle, R.J.2
  • 63
    • 0002832337 scopus 로고
    • Structure and function of allosteric enzymes
    • Data Trace Chem. Publ
    • 63. Lipscomb WN. 1991. Structure and function of allosteric enzymes. CHEMTRACTS-Biochem. Mol. Biol. [Data Trace Chem. Publ] 2:1-15
    • (1991) CHEMTRACTS-Biochem. Mol. Biol. , vol.2 , pp. 1-15
    • Lipscomb, W.N.1
  • 64
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteosome from the archaeon T. acidophilum at 3.4 Å resolution
    • 64. Lowe J, Stock D, Jap B, Zwickl P, Baumeister W, Huber R. 1995. Crystal structure of the 20S proteosome from the archaeon T. acidophilum at 3.4 Å resolution. Science 268:533-39
    • (1995) Science , vol.268 , pp. 533-539
    • Lowe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 65
    • 0014722597 scopus 로고
    • Enthalpyentropy compensation phenomena in water solutions of proteins and small molecules: A ubiquitous property of water
    • 65. Lumry R, Rajender S. 1970. Enthalpyentropy compensation phenomena in water solutions of proteins and small molecules: a ubiquitous property of water. Biopolymers 9:1125-227
    • (1970) Biopolymers , vol.9 , pp. 1125-1227
    • Lumry, R.1    Rajender, S.2
  • 66
    • 0026034515 scopus 로고
    • Modular organization of actin crosslinking proteins
    • 66. Matsudaira P. 1991. Modular organization of actin crosslinking proteins. Trends Biochem. Sci. 16:87-92
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 87-92
    • Matsudaira, P.1
  • 67
    • 0030444081 scopus 로고    scopus 로고
    • New structures of allosteric proteins revealing remarkable conformational changes
    • 67. Mattevi A, Rizzi M, Bolognesi M. 1996. New structures of allosteric proteins revealing remarkable conformational changes. Curr. Opin. Struct. Biol. 6:824-29
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 824-829
    • Mattevi, A.1    Rizzi, M.2    Bolognesi, M.3
  • 68
    • 0029645125 scopus 로고
    • Crystal structure of Escherichia coli pyruvate kinase type I: Molecular basis of the allosteric transition
    • 68. Mattevi A, Valentini G, Rizzi M, Speranza ML, Bolognesi M, Coda A. 1995. Crystal structure of Escherichia coli pyruvate kinase type I: molecular basis of the allosteric transition. Structure 3:729-41
    • (1995) Structure , vol.3 , pp. 729-741
    • Mattevi, A.1    Valentini, G.2    Rizzi, M.3    Speranza, M.L.4    Bolognesi, M.5    Coda, A.6
  • 69
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • 69. Mitchison T, Kirschner M. 1984. Dynamic instability of microtubule growth. Nature 312:237-42
    • (1984) Nature , vol.312 , pp. 237-242
    • Mitchison, T.1    Kirschner, M.2
  • 70
    • 0024155434 scopus 로고
    • Microtubule dynamics and kinetochore function in mitosis
    • 70. Mitchison TJ. 1988. Microtubule dynamics and kinetochore function in mitosis. Annu. Rev. Cell Biol. 4:527-49
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 527-549
    • Mitchison, T.J.1
  • 72
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • 72. Monod J, Wyman J, Changeux J-P. 1965. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12:88-118
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.-P.3
  • 73
    • 0016772655 scopus 로고
    • Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase
    • 73. Moras D, Olsen KW, Sabesan MN, Buehner M, Ford GC, Rossmann MG. 1975. Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 250:9137-62
    • (1975) J. Biol. Chem. , vol.250 , pp. 9137-9162
    • Moras, D.1    Olsen, K.W.2    Sabesan, M.N.3    Buehner, M.4    Ford, G.C.5    Rossmann, M.G.6
  • 74
    • 0021112807 scopus 로고
    • Structure of tomato bushy stunt virus IV. The virus particle at 2.9 Å resolution
    • 74. Olson AJ, Bricogne G, Harrison SC. 1983. Structure of tomato bushy stunt virus IV. The virus particle at 2.9 Å resolution. J. Mol. Biol. 171:61-93
    • (1983) J. Mol. Biol. , vol.171 , pp. 61-93
    • Olson, A.J.1    Bricogne, G.2    Harrison, S.C.3
  • 75
    • 0024722501 scopus 로고
    • Errors and alternatives in reading the universal genetic code
    • 75. Parker J. 1989. Errors and alternatives in reading the universal genetic code. Microbiol. Rev. 53:273-98
    • (1989) Microbiol. Rev. , vol.53 , pp. 273-298
    • Parker, J.1
  • 76
    • 0008435928 scopus 로고
    • Protein interactions: Aggregation of globular proteins
    • 76. Pauling L. 1953. Protein interactions: aggregation of globular proteins. Discov. Faraday Soc. 13:170-76
    • (1953) Discov. Faraday Soc. , vol.13 , pp. 170-176
    • Pauling, L.1
  • 77
    • 0017353813 scopus 로고
    • Morphogenetic core of the bacteriophage T4 head. Structure of the core in polyheads
    • 77. Paulson JR, Laemmli UK. 1977. Morphogenetic core of the bacteriophage T4 head. Structure of the core in polyheads. J. Mol. Biol. 111:459-85
    • (1977) J. Mol. Biol. , vol.111 , pp. 459-485
    • Paulson, J.R.1    Laemmli, U.K.2
  • 78
    • 2642600031 scopus 로고    scopus 로고
    • Human beta-trypsin is a ring-like tetramer with active sites facing a central pore
    • 78. Pereira PJB, Bergner A, Macedo-Ribeiro S, Huber R, Matxchiner G, et al. 1998. Human beta-trypsin is a ring-like tetramer with active sites facing a central pore. Nature 392:306-11
    • (1998) Nature , vol.392 , pp. 306-311
    • Pereira, P.J.B.1    Bergner, A.2    Macedo-Ribeiro, S.3    Huber, R.4    Matxchiner, G.5
  • 79
    • 0024953088 scopus 로고
    • Mechanisms of cooperativity and allosteric regulation in proteins
    • 79. Perutz MF. 1989. Mechanisms of cooperativity and allosteric regulation in proteins. Q. Rev. Biophys. 22:139-236
    • (1989) Q. Rev. Biophys. , vol.22 , pp. 139-236
    • Perutz, M.F.1
  • 80
    • 0025370816 scopus 로고
    • Structure-function relationships in dihydrolipoamide acyltransferases
    • 80. Reed LJ, Hackert ML. 1990. Structure-function relationships in dihydrolipoamide acyltransferases. J. Biol. Chem. 265:8971-74
    • (1990) J. Biol. Chem. , vol.265 , pp. 8971-8974
    • Reed, L.J.1    Hackert, M.L.2
  • 81
    • 0022418946 scopus 로고
    • Kinetic cooperativity of monomeric mnemonical enzymes
    • 81. Ricard J, Noat G. 1985. Kinetic cooperativity of monomeric mnemonical enzymes. Eur. J. Biochem. 152:557-64
    • (1985) Eur. J. Biochem. , vol.152 , pp. 557-564
    • Ricard, J.1    Noat, G.2
  • 82
    • 0021321202 scopus 로고
    • Constraints on the assembly of spherical virus particles
    • 82. Rossmann MG. 1984. Constraints on the assembly of spherical virus particles. Virology 134:1-11
    • (1984) Virology , vol.134 , pp. 1-11
    • Rossmann, M.G.1
  • 84
    • 0023364022 scopus 로고
    • Computer simulations of the diffusion of a substrate to an active site of an enzyme
    • 84. Sharp K, Fine R, Honig B. 1987. Computer simulations of the diffusion of a substrate to an active site of an enzyme. Science 236:1460-64
    • (1987) Science , vol.236 , pp. 1460-1464
    • Sharp, K.1    Fine, R.2    Honig, B.3
  • 85
    • 0025804295 scopus 로고
    • Crystal structure of a cholera toxin-related heat-labile enterotoxin from E. coli
    • 85. Sixma TK, Pronk SE, Kalk KH, Wartna ES, Zanten BAM, et al. 1991. Crystal structure of a cholera toxin-related heat-labile enterotoxin from E. coli. Nature 351:371-77
    • (1991) Nature , vol.351 , pp. 371-377
    • Sixma, T.K.1    Pronk, S.E.2    Kalk, K.H.3    Wartna, E.S.4    Zanten, B.A.M.5
  • 86
    • 0001885173 scopus 로고
    • Protein crystals as a model for mitochondrial proteins
    • 86. Srere PA. 1981. Protein crystals as a model for mitochondrial proteins. Trends Biochem. Sci. 6:4-7
    • (1981) Trends Biochem. Sci. , vol.6 , pp. 4-7
    • Srere, P.A.1
  • 87
    • 48549111326 scopus 로고
    • Why are enzymes so big?
    • 87. Srere PA. 1984. Why are enzymes so big? Trends Biochem. Sci. 9:387-90
    • (1984) Trends Biochem. Sci. , vol.9 , pp. 387-390
    • Srere, P.A.1
  • 88
    • 0024457508 scopus 로고
    • From signal to pseudopod: How cells control cytoplasmic actin assembly
    • 88. Stossel TP. 1989. From signal to pseudopod: How cells control cytoplasmic actin assembly. J. Biol. Chem. 264:18261-64
    • (1989) J. Biol. Chem. , vol.264 , pp. 18261-18264
    • Stossel, T.P.1
  • 89
    • 0029867028 scopus 로고    scopus 로고
    • Crystal structure of the T state of allosteric yeast chorismate mutase and comparison with the R state
    • 89. Strater N, Hakansson K, Schnappauf G, Braus G, Lipscomb WN. 1996. Crystal structure of the T state of allosteric yeast chorismate mutase and comparison with the R state. Proc. Natl. Acad. Sci. USA 93:3330-34
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3330-3334
    • Strater, N.1    Hakansson, K.2    Schnappauf, G.3    Braus, G.4    Lipscomb, W.N.5
  • 90
    • 0000829725 scopus 로고
    • Mass and size of protein molecules
    • 90. Svedberg T. 1929. Mass and size of protein molecules. Nature 123:871
    • (1929) Nature , vol.123 , pp. 871
    • Svedberg, T.1
  • 91
    • 0023067301 scopus 로고
    • Ferritin: Structure, gene regulation, and cellular function in animals, plants and microorganisms
    • 91. Theil EC. 1987. Ferritin: structure, gene regulation, and cellular function in animals, plants and microorganisms. Annu. Rev. Biochem. 56:289-315
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 289-315
    • Theil, E.C.1
  • 92
    • 0029790463 scopus 로고    scopus 로고
    • Intrinsic versus imposed curvature in cyclical oligomers: The portal protein of bacteriophage SPP1
    • 92. vanHeel M, Orlova EV, Dube P, Tavares P. 1996. Intrinsic versus imposed curvature in cyclical oligomers: the portal protein of bacteriophage SPP1. EMBO J. 15:4785-88
    • (1996) EMBO J. , vol.15 , pp. 4785-4788
    • VanHeel, M.1    Orlova, E.V.2    Dube, P.3    Tavares, P.4
  • 93
    • 0027200487 scopus 로고
    • Bacterial flagellar filaments and their component flagellins
    • 93. Wilson DR. 1993. Bacterial flagellar filaments and their component flagellins. Can. J. Microbiol. 39:451-72
    • (1993) Can. J. Microbiol. , vol.39 , pp. 451-472
    • Wilson, D.R.1
  • 94
    • 0027218692 scopus 로고
    • Structure-based inhibitors of HIV-1 protease
    • 94. Wlodawer A, Erickson JW. 1993. Structure-based inhibitors of HIV-1 protease. Annu. Rev. Biochem. 62:543-85
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 543-585
    • Wlodawer, A.1    Erickson, J.W.2
  • 95
    • 0029952910 scopus 로고    scopus 로고
    • Symmetry and the energy landscapes of biomolecules
    • 95. Wolynes PG. 1996. Symmetry and the energy landscapes of biomolecules. Proc. Natl. Acad. Sci. USA 93:14249-55
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14249-14255
    • Wolynes, P.G.1
  • 96
    • 0031913197 scopus 로고    scopus 로고
    • Mechanism and evolution of protein dimerization
    • 96. Xu D, Tsai C-J, Nussinov R. 1998. Mechanism and evolution of protein dimerization. Protein Sci. 7:533-44
    • (1998) Protein Sci. , vol.7 , pp. 533-544
    • Xu, D.1    Tsai, C.-J.2    Nussinov, R.3
  • 97
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    • 97. Xu Z, Horwich AL, Sigler PB. 1997. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 388:741-50
    • (1997) Nature , vol.388 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3
  • 98
    • 0031214216 scopus 로고    scopus 로고
    • Alanine-scanning mutagenesis of Bacillus subtilis trp RNA-binding attenuation protein (TRAP) reveals residues involved in tryptophan binding and RNA binding
    • 98. Yang M, Chen X-p, Militello K, Hoffman R, Fernandez B, et al. 1997. Alanine-scanning mutagenesis of Bacillus subtilis trp RNA-binding attenuation protein (TRAP) reveals residues involved in tryptophan binding and RNA binding. J. Mol. Biol. 270:696-710
    • (1997) J. Mol. Biol. , vol.270 , pp. 696-710
    • Yang, M.1    Chen, X.-P.2    Militello, K.3    Hoffman, R.4    Fernandez, B.5
  • 99
    • 0028205688 scopus 로고
    • Three-dimensional structure of the rotavirus haemagglutinin VP4 by cryo-electron microscopy and difference map analysis
    • 99. Yeager M, Berriman JA, Baker TS, Bellamy AR. 1994. Three-dimensional structure of the rotavirus haemagglutinin VP4 by cryo-electron microscopy and difference map analysis. EMBO J. 13:1011-18
    • (1994) EMBO J. , vol.13 , pp. 1011-1018
    • Yeager, M.1    Berriman, J.A.2    Baker, T.S.3    Bellamy, A.R.4
  • 101
    • 0008517524 scopus 로고    scopus 로고
    • note
    • 101. Protein Data Bank accession codes for structures used in the figures. The PDB may be reached at http://www.rcsb. org/pdb. Figure 1: pepsin, 5pep; alcohol dehydrogenase, 2ohx; porin, 2por; neuraminidase, 1ivb; phosphofructokinase, 1pfk; aspartate carbamoyltransferase, 1atl; glycolate oxidase, 1gox; glutamine synthetase, 2gls; protocatechuate-3,4-dioxygenase, 3pcg; ferritin, 1hrs; satellite tobacco necrosis virus, 2stv. Figure 2 superoxide dismutase, 1xso; interleukin 10, 1ilk. Figure 4: fructose-1,6-bisphosphatase, 4fbp (T) and 5fbp (R); aspartate carbamoyltransferase, 4atl (T) and 1atl (R). Figure 5: β subunit of RNA pol III, 2pol; PCNA, 1axc. Figure 6: GroEL, 1der; proteasome, 1ryp. Figure 7: satellite tobacco necrosis virus, 2stv; tomato bushy stunt virus, 2tbv. Figure 8: bluetongue virus, 2btv; simian virus 40, 1sva. Figure 11: hemoglobin, 4hhb. Figure 13: HIV-1 protease, 7hvp. Figure 14: GroEL:GroES, 1aon. Figure 16: reverse transcriptase, 3hvt.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.