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Volumn 137, Issue 1-2, 2002, Pages 54-64

Analysis of α-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation

Author keywords

Coiled coil; Computer program; Crick parameters; Heptad repeat; Protein conformation; Skips; Stutters

Indexed keywords

PROTEIN;

EID: 0036445512     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.2002.4454     Document Type: Conference Paper
Times cited : (220)

References (21)
  • 1
    • 0035967522 scopus 로고    scopus 로고
    • Buried polar residues in coiled-coil interfaces
    • Akey, D. L., Malashkevich, V. N., and Kim, P. S. (2001) Buried polar residues in coiled-coil interfaces. Biochemistry 40, 6352-6360.
    • (2001) Biochemistry , vol.40 , pp. 6352-6360
    • Akey, D.L.1    Malashkevich, V.N.2    Kim, P.S.3
  • 2
    • 0029957901 scopus 로고    scopus 로고
    • Heptad breaks in alpha-helical coiled coils: Stutters and stammers
    • Brown, J. H., Cohen, C., and Parry, D. A. (1996) Heptad breaks in alpha-helical coiled coils: Stutters and stammers. Proteins 26, 134-145.
    • (1996) Proteins , vol.26 , pp. 134-145
    • Brown, J.H.1    Cohen, C.2    Parry, D.A.3
  • 3
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough, P. A., Hughson, F. M., Skehel, J. J., and Wiley, D. C. (1994) Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371, 37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 4
    • 0034653908 scopus 로고    scopus 로고
    • The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of inter- and intra-helical salt-bridges
    • Burkhard, P., Kammerer, R. A., Steinmetz, M. O., Bourenkov, G. P., and Aebi, U. (2000) The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of inter- and intra-helical salt-bridges. Structure 8, 223-230.
    • (2000) Structure , vol.8 , pp. 223-230
    • Burkhard, P.1    Kammerer, R.A.2    Steinmetz, M.O.3    Bourenkov, G.P.4    Aebi, U.5
  • 5
    • 0035252931 scopus 로고    scopus 로고
    • Coiled coils: A highly versatile protein folding motif
    • Burkhard, P., Stetefeld, J., and Strelkov, S. V. (2001) Coiled coils: A highly versatile protein folding motif. Trends Cell. Biol. 11, 82-8.
    • (2001) Trends Cell. Biol. , vol.11 , pp. 82-88
    • Burkhard, P.1    Stetefeld, J.2    Strelkov, S.V.3
  • 6
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (1994) The CCP4 suite: Programs for protein crystallography. Acta Cryst. D50, 760-763.
    • (1994) Acta Cryst. , vol.D50 , pp. 760-763
  • 7
  • 8
    • 0001105482 scopus 로고
    • Is alpha-keratin a coiled coil?
    • Crick, F. H. C. (1952) Is alpha-keratin a coiled coil? Nature 170, 882-883.
    • (1952) Nature , vol.170 , pp. 882-883
    • Crick, F.H.C.1
  • 9
    • 0000747247 scopus 로고
    • The Fourier transform of a coiled-coil
    • Crick, F. H. C. (1953) The Fourier transform of a coiled-coil. Acta Crystallogr. 6, 685-689.
    • (1953) Acta Crystallogr. , vol.6 , pp. 685-689
    • Crick, F.H.C.1
  • 10
    • 0027934571 scopus 로고
    • Crystal structure of an isoleucine-zipper trimer
    • Harbury, P. B., Kim, P. S., and Alber, T. (1994) Crystal structure of an isoleucine-zipper trimer. Nature 371, 80-83.
    • (1994) Nature , vol.371 , pp. 80-83
    • Harbury, P.B.1    Kim, P.S.2    Alber, T.3
  • 11
    • 0034669204 scopus 로고    scopus 로고
    • Crystal structure of the Xrcc4 DNA repair protein and implications for end joining
    • Junop, M. S., Modesti, M., Guarne, A., Ghirlando, R., Gellert, M., and Yang, W. (2000) Crystal structure of the Xrcc4 DNA repair protein and implications for end joining. EMBO J. 19, 5962-5970.
    • (2000) EMBO J. , vol.19 , pp. 5962-5970
    • Junop, M.S.1    Modesti, M.2    Guarne, A.3    Ghirlando, R.4    Gellert, M.5    Yang, W.6
  • 12
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: New structures and new functions
    • Lupas, A. (1996) Coiled coils: New structures and new functions. Trends Biochem. Sci. 21, 375-382.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 375-382
    • Lupas, A.1
  • 13
    • 0030960276 scopus 로고    scopus 로고
    • Predicting coiled-coil regions in proteins
    • Lupas, A. (1997) Predicting coiled-coil regions in proteins. Curr. Opin. Struct. Biol. 7, 388-393.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 388-393
    • Lupas, A.1
  • 14
    • 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., and Alber, T. (1991) X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science 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
  • 15
    • 0027532105 scopus 로고
    • Pitch diversity in alpha-helical coiled coils
    • Seo, J., and Cohen, C. (1993) Pitch diversity in alpha-helical coiled coils. Proteins 15, 223-234.
    • (1993) Proteins , vol.15 , pp. 223-234
    • Seo, J.1    Cohen, C.2
  • 18
    • 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., Aebi, U., and Burkhard, P. (2002) Conserved segments 1A and 2B of the intermediate filament dimer: Their atomic structures and role in filament assembly. EMBO J. 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    Aebi, U.6    Burkhard, P.7
  • 19
    • 0031570687 scopus 로고    scopus 로고
    • Structure of bacteriophage T4 fibritin: A segmented coiled coil and the role of the C-terminal domain
    • Tao, Y., Strelkov, S. V., Mesyanzhinov, V. V., and Rossmann, M. G. (1997) Structure of bacteriophage T4 fibritin: A segmented coiled coil and the role of the C-terminal domain. Structure 5, 789-798.
    • (1997) Structure , vol.5 , pp. 789-798
    • Tao, Y.1    Strelkov, S.V.2    Mesyanzhinov, V.V.3    Rossmann, M.G.4
  • 20
    • 0035853291 scopus 로고    scopus 로고
    • Socket: A program for identifying and analysing coiled-coil motifs within protein structures
    • Walshaw, J., and Woolfson, D. N. (2001) Socket: A program for identifying and analysing coiled-coil motifs within protein structures. J. Mol. Biol. 307, 1427-1450.
    • (2001) J. Mol. Biol. , vol.307 , pp. 1427-1450
    • Walshaw, J.1    Woolfson, D.N.2
  • 21
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution
    • Wilson, I. A., Skehel, J. J., and Wiley, D. C. (1981) Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature 289, 366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.