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Volumn 50, Issue 2, 2003, Pages 207-212

Modeling α-helical coiled-coil interactions: The axial and azimuthal alignment of 1B segments from vimentin intermediate filaments

Author keywords

fibrous proteins; Assembly mechanics; Coiled coils; Energetics of assembly; Intermediate filaments; Ionic residue periodicity; Stabilization of protein assemblies; Vimentin

Indexed keywords

AMINO ACID; M PROTEIN; VIMENTIN;

EID: 0037297399     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10254     Document Type: Article
Times cited : (9)

References (29)
  • 2
    • 0019873745 scopus 로고
    • Structure of rabbit skeletal myosin: Analysis of the amino acid sequence of two fragments from the rod region
    • Parry DAD. Structure of rabbit skeletal myosin: Analysis of the amino acid sequence of two fragments from the rod region. J Mol Biol 1981;153:459-464.
    • (1981) J Mol Biol , vol.153 , pp. 459-464
    • Parry, D.A.D.1
  • 3
    • 0021103673 scopus 로고
    • Periodic features in the amino acid sequence of nematode myosin rod
    • McLachlan AD, Karn J. Periodic features in the amino acid sequence of nematode myosin rod. J Mol Biol 1983;164:605-626.
    • (1983) J Mol Biol , vol.164 , pp. 605-626
    • McLachlan, A.D.1    Karn, J.2
  • 4
    • 0023279460 scopus 로고
    • Amino acid sequence and structural repeats in schistosome paramyosin match those of myosin
    • Cohen C, Lanar DE, Parry DAD. Amino acid sequence and structural repeats in schistosome paramyosin match those of myosin. Biosci Rep 1987;7:11-16.
    • (1987) Biosci Rep , vol.7 , pp. 11-16
    • Cohen, C.1    Lanar, D.E.2    Parry, D.A.D.3
  • 5
    • 0024974671 scopus 로고
    • Paramyosin gene (unc-15) of Caenorhabditis elegans: Molecular cloning, nucleotide sequence and models for thick filament structure
    • Kagawa H, Gengyo K, McLachlan AD, Brenner S, Karn J. Paramyosin gene (unc-15) of Caenorhabditis elegans: Molecular cloning, nucleotide sequence and models for thick filament structure. J Mol Biol 1989;207:311-333.
    • (1989) J Mol Biol , vol.207 , pp. 311-333
    • Kagawa, H.1    Gengyo, K.2    McLachlan, A.D.3    Brenner, S.4    Karn, J.5
  • 6
    • 0017379297 scopus 로고
    • Structure of α-keratin: Structural implication of the amino acid sequences of the type I and type II chain segments
    • Parry DAD, Crewther WG, Fraser RDB, MacRae TP. Structure of α-keratin: Structural implication of the amino acid sequences of the type I and type II chain segments. J Mol Biol 1977;113:449-454.
    • (1977) J Mol Biol , vol.113 , pp. 449-454
    • Parry, D.A.D.1    Crewther, W.G.2    Fraser, R.D.B.3    MacRae, T.P.4
  • 7
    • 0020484490 scopus 로고
    • Periodic charge distribution in the intermediate filament proteins desmin and vimentin
    • McLachlan AD, Stewart M. Periodic charge distribution in the intermediate filament proteins desmin and vimentin. J Mol Biol 1982;162:693-698.
    • (1982) J Mol Biol , vol.162 , pp. 693-698
    • McLachlan, A.D.1    Stewart, M.2
  • 8
  • 10
    • 0026510756 scopus 로고
    • Analysis of the three-α-helix motif in the spectrin superfamily of proteins
    • Parry DAD, Dixon TW, Cohen C. Analysis of the three-α-helix motif in the spectrin superfamily of proteins. Biophys J 1992;61:858-867.
    • (1992) Biophys J , vol.61 , pp. 858-867
    • Parry, D.A.D.1    Dixon, T.W.2    Cohen, C.3
  • 11
    • 0028283501 scopus 로고
    • Intermediate filament structure, dynamics, function and disease
    • Fuchs E, Weber K. Intermediate filament structure, dynamics, function and disease. Annu Rev Biochem 1994;63:345-382.
    • (1994) Annu Rev Biochem , vol.63 , pp. 345-382
    • Fuchs, E.1    Weber, K.2
  • 13
    • 0032053588 scopus 로고    scopus 로고
    • Intermediate filament assembly: Fibrillogenesis is driven by decisive dimer-dimer interactions
    • Herrmann H, Aebi U. Intermediate filament assembly: Fibrillogenesis is driven by decisive dimer-dimer interactions. Curr Opin Struct Biol 1998;8:177-185.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 177-185
    • Herrmann, H.1    Aebi, U.2
  • 14
    • 0027160195 scopus 로고
    • Keratin intermediate filament structure: Crosslinking studies yield quantitative information on molecular dimensions and mechanism of assembly
    • Steinert PM, Marekov LN, Fraser RDB, Parry DAD. Keratin intermediate filament structure: Crosslinking studies yield quantitative information on molecular dimensions and mechanism of assembly. J Mol Biol 1993;230:436-452.
    • (1993) J Mol Biol , vol.230 , pp. 436-452
    • Steinert, P.M.1    Marekov, L.N.2    Fraser, R.D.B.3    Parry, D.A.D.4
  • 15
    • 0027501845 scopus 로고
    • Conservation of the structure of keratin intermediate filaments: Molecular mechanism by which different keratin molecules integrate into preexisting keratin intermediate filaments during differentiation
    • Steinert PM, Marekov LN, Parry DAD. Conservation of the structure of keratin intermediate filaments: Molecular mechanism by which different keratin molecules integrate into preexisting keratin intermediate filaments during differentiation. Biochemistry 1993;32:10046-10056.
    • (1993) Biochemistry , vol.32 , pp. 10046-10056
    • Steinert, P.M.1    Marekov, L.N.2    Parry, D.A.D.3
  • 16
    • 0027435278 scopus 로고
    • Diversity of intermediate filament structure: Evidence that the alignment of coiled-coil molecules in vimentin is different from that in keratin intermediate filaments
    • Steinert PM, Marekov LN, Parry DAD. Diversity of intermediate filament structure: Evidence that the alignment of coiled-coil molecules in vimentin is different from that in keratin intermediate filaments. J Biol Chem 1993;268:24916-24925.
    • (1993) J Biol Chem , vol.268 , pp. 24916-24925
    • Steinert, P.M.1    Marekov, L.N.2    Parry, D.A.D.3
  • 17
    • 0035914358 scopus 로고    scopus 로고
    • Sub-filamentous protofibril structures in fibrous proteins: Cross-linking evidence for protofibrils in intermediate filaments
    • Parry DAD, Marekov LN, Steinert PM. Sub-filamentous protofibril structures in fibrous proteins: Cross-linking evidence for protofibrils in intermediate filaments. J Biol Chem 2001;276:39253-39258.
    • (2001) J Biol Chem , vol.276 , pp. 39253-39258
    • Parry, D.A.D.1    Marekov, L.N.2    Steinert, P.M.3
  • 18
    • 0033555523 scopus 로고    scopus 로고
    • Molecular parameters of type IV α-internexin and type IV-type III α-internexin-vimentin copolymer intermediate filaments
    • Steinert PM, Marekov LN, Parry DAD. Molecular parameters of type IV α-internexin and type IV-type III α-internexin-vimentin copolymer intermediate filaments. J Biol Chem 1999;274:1657-1666.
    • (1999) J Biol Chem , vol.274 , pp. 1657-1666
    • Steinert, P.M.1    Marekov, L.N.2    Parry, D.A.D.3
  • 19
    • 0033498452 scopus 로고    scopus 로고
    • Intermediate filaments: Molecular architecture, assembly, dynamics and polymorphism
    • Parry DAD, Steinert PM. Intermediate filaments: Molecular architecture, assembly, dynamics and polymorphism. Q Rev Biophys 1999;32:99-187.
    • (1999) Q Rev Biophys , vol.32 , pp. 99-187
    • Parry, D.A.D.1    Steinert, P.M.2
  • 20
    • 0034739847 scopus 로고    scopus 로고
    • In vitro assembly and structure of trichocyte keratin intermediate filaments: A novel role for stabilization by disulfide bonding
    • Wang H, Parry DAD, Jones LN, Idler WW, Marekov LN, Steinert PM. In vitro assembly and structure of trichocyte keratin intermediate filaments: A novel role for stabilization by disulfide bonding. J Cell Biol 2000;151:1459-1468.
    • (2000) J Cell Biol , vol.151 , pp. 1459-1468
    • Wang, H.1    Parry, D.A.D.2    Jones, L.N.3    Idler, W.W.4    Marekov, L.N.5    Steinert, P.M.6
  • 21
    • 0018637473 scopus 로고
    • Repeating patterns of amino acid residues in the sequences of some high-sulphur proteins from α-keratin
    • Parry DAD, Fraser RDB, MacRae TP. Repeating patterns of amino acid residues in the sequences of some high-sulphur proteins from α-keratin. Int J Biol Macromol 1979;1:17-22.
    • (1979) Int J Biol Macromol , vol.1 , pp. 17-22
    • Parry, D.A.D.1    Fraser, R.D.B.2    MacRae, T.P.3
  • 22
    • 0029902659 scopus 로고    scopus 로고
    • Hard α-keratin intermediate filaments: An alternative interpretation of the low-angle equatorial X-ray diffraction pattern, and the axial disposition of putative disulphide bonds in the intra- and inter-protofilamentous networks
    • Parry DAD. Hard α-keratin intermediate filaments: An alternative interpretation of the low-angle equatorial X-ray diffraction pattern, and the axial disposition of putative disulphide bonds in the intra- and inter-protofilamentous networks Int J Biol Macromol 1996;19:45-50.
    • (1996) Int J Biol Macromol , vol.19 , pp. 45-50
    • Parry, D.A.D.1
  • 23
    • 0034685607 scopus 로고    scopus 로고
    • The intermediate filament protein consensus motif of helix 2B: Its atomic structure and contribution to assembly
    • Herrmann H, Strelkov SV, Feja B, et al. The intermediate filament protein consensus motif of helix 2B: Its atomic structure and contribution to assembly. J Mol Biol 2000;298:817-832.
    • (2000) J Mol Biol , vol.298 , pp. 817-832
    • Herrmann, H.1    Strelkov, S.V.2    Feja, B.3
  • 24
    • 0037086445 scopus 로고    scopus 로고
    • Conserved segments 1A and 2B of the intermediate filament dimer: Their atomic structures and role in filament assembly
    • Strelkov SV, Herrmann H, Geisler N, et al. Conserved segments 1A and 2B of the intermediate filament dimer: Their atomic structures and role in filament assembly. EMBO J 2002;21:1255-1266.
    • (2002) EMBO J , vol.21 , pp. 1255-1266
    • Strelkov, S.V.1    Herrmann, H.2    Geisler, N.3
  • 25
    • 0003978919 scopus 로고    scopus 로고
    • July 1998 release b, license CNRS/Universite Aix-Marseille II, Roussel A, Cambillau C. AFMBIFRC1 chemin J. Aiguier 13402 Marseille, France, FTP anonymous: afmb.cnrs-mrs.fr or 194.214.212
    • Roussel A, Inisan AG, Knoops-Mouthuy E, Cambilau C. TURBOFRODO Version OpenGL.1, July 1998 release b (1998), license CNRS/Universite Aix-Marseille II, Roussel A, Cambillau C. AFMBIFRC1 chemin J. Aiguier 13402 Marseille, France. Web page: http://afmb.cnrs-mrs.fr/TURBO FRODO/turbo.html., FTP anonymous: afmb.cnrs-mrs.fr or 194.214.212.50.
    • (1998) TURBOFRODO Version OpenGL.1
    • Roussel, A.1    Inisan, A.G.2    Knoops-Mouthuy, E.3    Cambilau, C.4
  • 28
    • 0027476386 scopus 로고
    • The conserved H1 domain of the type II keratin 1 chain plays an essential role in the alignment of nearest-neighbor molecules in mouse and human keratin 1/keratin 10 intermediate filaments at the two- to four-molecule level of structure
    • Steinert PM, Parry DAD. The conserved H1 domain of the type II keratin 1 chain plays an essential role in the alignment of nearest-neighbor molecules in mouse and human keratin 1/keratin 10 intermediate filaments at the two- to four-molecule level of structure. J Biol Chem 1993;268:2878-2887.
    • (1993) J Biol Chem , vol.268 , pp. 2878-2887
    • Steinert, P.M.1    Parry, D.A.D.2
  • 29
    • 0028290358 scopus 로고
    • Function of type I and type II keratin head domains: Their role in dimer, tetramer and filament formation
    • Hatzfeld M, Burba M. Function of type I and type II keratin head domains: Their role in dimer, tetramer and filament formation. J Cell Sci 1994;107:1959-1972.
    • (1994) J Cell Sci , vol.107 , pp. 1959-1972
    • Hatzfeld, M.1    Burba, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.