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Volumn 177, Issue 1, 2012, Pages 46-53

Stabilization of vimentin coil2 fragment via an engineered disulfide

Author keywords

Coiled coil; Crystallization; Dimerization; Engineered disulfide; Intermediate filaments

Indexed keywords

CYSTEINE; DISULFIDE; INTERMEDIATE FILAMENT PROTEIN; VIMENTIN;

EID: 84855839529     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2011.11.014     Document Type: Article
Times cited : (27)

References (40)
  • 2
    • 0002344099 scopus 로고
    • Unifying principles in intermediate filament structure and assembly
    • Aebi U., Haner M., Troncoso J., Eichner R., Engel A. Unifying principles in intermediate filament structure and assembly. Protoplasma 1988, 145:73-81.
    • (1988) Protoplasma , vol.145 , pp. 73-81
    • Aebi, U.1    Haner, M.2    Troncoso, J.3    Eichner, R.4    Engel, A.5
  • 3
    • 0035252931 scopus 로고    scopus 로고
    • Coiled coils: a highly versatile protein folding motif
    • Burkhard P., Stetefeld J., Strelkov S.V. Coiled coils: a highly versatile protein folding motif. Trends Cell Biol. 2001, 11:82-88.
    • (2001) Trends Cell Biol. , vol.11 , pp. 82-88
    • Burkhard, P.1    Stetefeld, J.2    Strelkov, S.V.3
  • 4
    • 0001280314 scopus 로고
    • Biosynthesis by Escherichia coli of active altered proteins containing selenium instead of sulfur
    • Cowie D.B., Cohen G.N. Biosynthesis by Escherichia coli of active altered proteins containing selenium instead of sulfur. Biochim. Biophys. Acta 1957, 26:252-261.
    • (1957) Biochim. Biophys. Acta , vol.26 , pp. 252-261
    • Cowie, D.B.1    Cohen, G.N.2
  • 5
    • 84873069986 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System DeLano Scientific, San Carlos, CA, USA. Availble from: <>.
    • DeLano, W.L. 2002. The PyMOL Molecular Graphics System DeLano Scientific, San Carlos, CA, USA. Availble from: <>. http://www.pymol.org.
    • (2002)
    • DeLano, W.L.1
  • 7
    • 0344628627 scopus 로고    scopus 로고
    • Historical review: another 50th anniversary - new periodicities in coiled coils
    • Gruber M., Lupas A.N. Historical review: another 50th anniversary - new periodicities in coiled coils. Trends Biochem. Sci. 2003, 28:679-685.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 679-685
    • Gruber, M.1    Lupas, A.N.2
  • 8
    • 0025239701 scopus 로고
    • The coiled coil of in vitro assembled keratin filaments is a heterodimer of type I and II keratins: use of site-specific mutagenesis and recombinant protein expression
    • Hatzfeld M., Weber K. The coiled coil of in vitro assembled keratin filaments is a heterodimer of type I and II keratins: use of site-specific mutagenesis and recombinant protein expression. J. Cell Biol. 1990, 110:1199-1210.
    • (1990) J. Cell Biol. , vol.110 , pp. 1199-1210
    • Hatzfeld, M.1    Weber, K.2
  • 9
    • 3943078618 scopus 로고    scopus 로고
    • Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds
    • Herrmann H., Aebi U. Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds. Annu. Rev. Biochem. 2004, 73:749-789.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 749-789
    • Herrmann, H.1    Aebi, U.2
  • 11
    • 0034685607 scopus 로고    scopus 로고
    • The intermediate filament protein consensus motif of helix 2B: its atomic structure and contribution to assembly
    • Herrmann H., Strelkov S.V., Feja B., Rogers K.R., Brettel M., 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    Rogers, K.R.4    Brettel, M.5
  • 12
    • 0035909890 scopus 로고    scopus 로고
    • Side-chain repacking calculations for predicting structures and stabilities of heterodimeric coiled coils
    • Keating A.E., Malashkevich V.N., Tidor B., Kim P.S. Side-chain repacking calculations for predicting structures and stabilities of heterodimeric coiled coils. Proc. Natl. Acad. Sci. USA 2001, 98:14825-14830.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14825-14830
    • Keating, A.E.1    Malashkevich, V.N.2    Tidor, B.3    Kim, P.S.4
  • 13
    • 10344236049 scopus 로고    scopus 로고
    • The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat
    • Kuhnel K., Jarchau T., Wolf E., Schlichting I., Walter U., et al. The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat. Proc. Natl. Acad. Sci. USA 2004, 101:17027-17032.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 17027-17032
    • Kuhnel, K.1    Jarchau, T.2    Wolf, E.3    Schlichting, I.4    Walter, U.5
  • 14
    • 2442655493 scopus 로고    scopus 로고
    • Stabilizing and destabilizing clusters in the hydrophobic core of long two-stranded alpha-helical coiled-coils
    • Kwok S.C., Hodges R.S. Stabilizing and destabilizing clusters in the hydrophobic core of long two-stranded alpha-helical coiled-coils. J. Biol. Chem. 2004, 279:21576-21588.
    • (2004) J. Biol. Chem. , vol.279 , pp. 21576-21588
    • Kwok, S.C.1    Hodges, R.S.2
  • 15
    • 45349085365 scopus 로고    scopus 로고
    • Expression and purification of cysteine mutation isoforms of rat lipocalin-type prostaglandin D synthase for nuclear magnetic resonance study
    • Liu J., Lin K., Guo C., Gao H., Yao Y., et al. Expression and purification of cysteine mutation isoforms of rat lipocalin-type prostaglandin D synthase for nuclear magnetic resonance study. Acta Biochim. Biophys. Sin. (Shanghai) 2008, 40:489-496.
    • (2008) Acta Biochim. Biophys. Sin. (Shanghai) , vol.40 , pp. 489-496
    • Liu, J.1    Lin, K.2    Guo, C.3    Gao, H.4    Yao, Y.5
  • 16
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas A., Van Dyke M., Stock J. Predicting coiled coils from protein sequences. Science 1991, 252:1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 19
    • 67349199644 scopus 로고    scopus 로고
    • Vimentin coil 1A-A molecular switch involved in the initiation of filament elongation
    • Meier M., Padilla G.P., Herrmann H., Wedig T., Hergt M., et al. Vimentin coil 1A-A molecular switch involved in the initiation of filament elongation. J. Mol. Biol. 2009, 390:245-261.
    • (2009) J. Mol. Biol. , vol.390 , pp. 245-261
    • Meier, M.1    Padilla, G.P.2    Herrmann, H.3    Wedig, T.4    Hergt, M.5
  • 20
    • 0026025936 scopus 로고
    • Kinetics of self-assembly of alpha alpha-tropomyosin coiled coils from unfolded chains
    • Mo J.M., Holtzer M.E., Holtzer A. Kinetics of self-assembly of alpha alpha-tropomyosin coiled coils from unfolded chains. Proc. Natl. Acad. Sci. USA 1991, 88:916-920.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 916-920
    • Mo, J.M.1    Holtzer, M.E.2    Holtzer, A.3
  • 22
    • 0027949066 scopus 로고
    • Coiled-coil stutter and link segments in keratin and other intermediate filament molecules: a computer modeling study
    • North A.C., Steinert P.M., Parry D.A. Coiled-coil stutter and link segments in keratin and other intermediate filament molecules: a computer modeling study. Proteins 1994, 20:174-184.
    • (1994) Proteins , vol.20 , pp. 174-184
    • North, A.C.1    Steinert, P.M.2    Parry, D.A.3
  • 23
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • O'Shea E.K., Klemm J.D., Kim P.S., Alber T. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science 1991, 254:539-544.
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 24
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 1997, 277:307-325.
    • (1997) Methods Enzymol. , vol.277 , pp. 307-325
    • Otwinowski, Z.1    Minor, W.2
  • 25
    • 0025019350 scopus 로고
    • Conformational stability of globular proteins
    • Pace C.N. Conformational stability of globular proteins. Trends Biochem. Sci. 1990, 15:14-17.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 14-17
    • Pace, C.N.1
  • 26
    • 0031808074 scopus 로고    scopus 로고
    • A helix propensity scale based on experimental studies of peptides and proteins
    • Pace C.N., Scholtz J.M. A helix propensity scale based on experimental studies of peptides and proteins. Biophys. J. 1998, 75:422-427.
    • (1998) Biophys. J. , vol.75 , pp. 422-427
    • Pace, C.N.1    Scholtz, J.M.2
  • 27
    • 23844492576 scopus 로고    scopus 로고
    • Auto-Rickshaw: an automated crystal structure determination platform as an efficient tool for the validation of an X-ray diffraction experiment
    • Panjikar S., Parthasarathy V., Lamzin V.S., Weiss M.S., Tucker P.A. Auto-Rickshaw: an automated crystal structure determination platform as an efficient tool for the validation of an X-ray diffraction experiment. Acta Crystallogr. D Biol. Crystallogr. 2005, 61:449-457.
    • (2005) Acta Crystallogr. D Biol. Crystallogr. , vol.61 , pp. 449-457
    • Panjikar, S.1    Parthasarathy, V.2    Lamzin, V.S.3    Weiss, M.S.4    Tucker, P.A.5
  • 28
    • 33747768593 scopus 로고    scopus 로고
    • Hendecad repeat in segment 2A and linker L2 of intermediate filament chains implies the possibility of a right-handed coiled-coil structure
    • Parry D.A. Hendecad repeat in segment 2A and linker L2 of intermediate filament chains implies the possibility of a right-handed coiled-coil structure. J. Struct. Biol. 2006, 155:370-374.
    • (2006) J. Struct. Biol. , vol.155 , pp. 370-374
    • Parry, D.A.1
  • 29
    • 34547930859 scopus 로고    scopus 로고
    • Complete maps of molecular-loop conformational spaces
    • Porta J.M., Ros L., Thomas F., Corcho F., Canto J., et al. Complete maps of molecular-loop conformational spaces. J. Comput. Chem. 2007, 28:2170-2189.
    • (2007) J. Comput. Chem. , vol.28 , pp. 2170-2189
    • Porta, J.M.1    Ros, L.2    Thomas, F.3    Corcho, F.4    Canto, J.5
  • 30
    • 0030198631 scopus 로고    scopus 로고
    • Characterization of disulfide crosslink formation of human vimentin at the dimer, tetramer, and intermediate filament levels
    • Rogers K.R., Herrmann H., Franke W.W. Characterization of disulfide crosslink formation of human vimentin at the dimer, tetramer, and intermediate filament levels. J. Struct. Biol. 1996, 117:55-69.
    • (1996) J. Struct. Biol. , vol.117 , pp. 55-69
    • Rogers, K.R.1    Herrmann, H.2    Franke, W.W.3
  • 33
    • 0036445512 scopus 로고    scopus 로고
    • Analysis of alpha-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation
    • Strelkov S.V., Burkhard P. Analysis of alpha-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation. J. Struct. Biol. 2002, 137:54-64.
    • (2002) J. Struct. Biol. , vol.137 , pp. 54-64
    • Strelkov, S.V.1    Burkhard, P.2
  • 34
    • 0037335755 scopus 로고    scopus 로고
    • Molecular architecture of intermediate filaments
    • Strelkov S.V., Herrmann H., Aebi U. Molecular architecture of intermediate filaments. BioEssays 2003, 25:243-251.
    • (2003) BioEssays , vol.25 , pp. 243-251
    • Strelkov, S.V.1    Herrmann, H.2    Aebi, U.3
  • 36
    • 5144220584 scopus 로고    scopus 로고
    • Crystal structure of the human lamin A coil 2B dimer: implications for the head-to-tail association of nuclear lamins
    • Strelkov S.V., Schumacher J., Burkhard P., Aebi U., Herrmann H. Crystal structure of the human lamin A coil 2B dimer: implications for the head-to-tail association of nuclear lamins. J. Mol. Biol. 2004, 343:1067-1080.
    • (2004) J. Mol. Biol. , vol.343 , pp. 1067-1080
    • Strelkov, S.V.1    Schumacher, J.2    Burkhard, P.3    Aebi, U.4    Herrmann, H.5
  • 37
    • 0037086445 scopus 로고    scopus 로고
    • Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly
    • Strelkov S.V., Herrmann H., Geisler N., Wedig T., Zimbelmann R., 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    Wedig, T.4    Zimbelmann, R.5
  • 38
    • 0035793704 scopus 로고    scopus 로고
    • Divide-and-conquer crystallographic approach towards an atomic structure of intermediate filaments
    • Strelkov S.V., Herrmann H., Geisler N., Lustig A., Ivaninskii S., et al. Divide-and-conquer crystallographic approach towards an atomic structure of intermediate filaments. J. Mol. Biol. 2001, 306:773-781.
    • (2001) J. Mol. Biol. , vol.306 , pp. 773-781
    • Strelkov, S.V.1    Herrmann, H.2    Geisler, N.3    Lustig, A.4    Ivaninskii, S.5
  • 39
    • 0035853291 scopus 로고    scopus 로고
    • Socket: a program for identifying and analysing coiled-coil motifs within protein structures
    • Walshaw J., Woolfson D.N. Socket: a program for identifying and analysing coiled-coil motifs within protein structures. J. Mol. Biol. 2001, 307:1427-1450.
    • (2001) J. Mol. Biol. , vol.307 , pp. 1427-1450
    • Walshaw, J.1    Woolfson, D.N.2
  • 40
    • 0027480940 scopus 로고
    • Disulfide bond contribution to protein stability: positional effects of substitution in the hydrophobic core of the two-stranded alpha-helical coiled-coil
    • Zhou N.E., Kay C.M., Hodges R.S. Disulfide bond contribution to protein stability: positional effects of substitution in the hydrophobic core of the two-stranded alpha-helical coiled-coil. Biochemistry 1993, 32:3178-3187.
    • (1993) Biochemistry , vol.32 , pp. 3178-3187
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.