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Volumn 2, Issue 3, 1997, Pages 149-158

Coiled-coil assembly by peptides with non-heptad sequence motifs

Author keywords

Circular dichroism; Hendecad; Peptide models; Protein folding; Protein structure; Undecatad

Indexed keywords

CYTOSKELETON PROTEIN; PEPTIDE; PROTOZOAL PROTEIN;

EID: 0030624409     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(97)00021-7     Document Type: Article
Times cited : (57)

References (48)
  • 1
    • 0000920828 scopus 로고
    • The packing of α-helices: Simple coiled-coils
    • Crick, F.H.C. (1953). The packing of α-helices: simple coiled-coils. Acta. Crystallogr. 6, 689-697.
    • (1953) Acta. Crystallogr. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 2
    • 0024961717 scopus 로고
    • Sequence-analysis of the complete Caenorhabditis elegans myosin heavy-chain gene family
    • Dibb, N.J., Maruyama, I.N., Krause, M. & Karn, J. (1989). Sequence-analysis of the complete Caenorhabditis elegans myosin heavy-chain gene family. J. Mol. Biol. 205, 603-613.
    • (1989) J. Mol. Biol. , vol.205 , pp. 603-613
    • Dibb, N.J.1    Maruyama, I.N.2    Krause, M.3    Karn, J.4
  • 3
    • 0024534241 scopus 로고
    • Evidence that the leucine zipper is a coiled coil
    • O'Shea, E.K., Rutkowski, R. & Kim, P.S. (1989). Evidence that the leucine zipper is a coiled coil. Science 243, 538-542.
    • (1989) Science , vol.243 , pp. 538-542
    • O'Shea, E.K.1    Rutkowski, R.2    Kim, P.S.3
  • 5
    • 0016774265 scopus 로고
    • Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure
    • McLachlan, A.D. & Stewart, M. (1975). Tropomyosin coiled-coil interactions: evidence for an unstaggered structure. J. Mol. Biol. 98, 293-304.
    • (1975) J. Mol. Biol. , vol.98 , pp. 293-304
    • McLachlan, A.D.1    Stewart, M.2
  • 6
    • 0002732819 scopus 로고
    • Compound helical configurations of polypeptide chains: Structure of proteins of the α-keratin type
    • Pauling, L. & Corey, E.B. (1953). Compound helical configurations of polypeptide chains: structure of proteins of the α-keratin type. Nature 171, 59-61.
    • (1953) Nature , vol.171 , pp. 59-61
    • Pauling, L.1    Corey, E.B.2
  • 7
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
    • Wilson, I.A., Skehel, J.J. & Wiley, D.C. (1981). Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature 289, 366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 8
    • 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. (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
  • 9
    • 0027934571 scopus 로고
    • Crystal structure of an isoleucine-zipper trimer
    • Harbury, P.B., Kim, P.S. & 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
  • 10
    • 0027756896 scopus 로고
    • A switch between two-, three- and four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury, P.B., Zhang, T., Kim, P.S. & Alber, T. (1993). A switch between two-, three- and four-stranded coiled coils in GCN4 leucine zipper mutants. Science 262, 1401-1407.
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 11
    • 0025130161 scopus 로고
    • Structural features in the heptad substructures and longer range repeats of two-stranded α-fibrous proteins
    • Conway, J.F. & Parry, D.A.D. (1990). Structural features in the heptad substructures and longer range repeats of two-stranded α-fibrous proteins. Int. J. Biol. Macromol. 12, 328-334.
    • (1990) Int. J. Biol. Macromol. , vol.12 , pp. 328-334
    • Conway, J.F.1    Parry, D.A.D.2
  • 12
    • 0026028894 scopus 로고
    • Three-stranded α-fibrous proteins: The heptad repeat and its implications for structure
    • Conway, J.F. & Parry, D.A.D. (1991). Three-stranded α-fibrous proteins: the heptad repeat and its implications for structure. Int. J. Biol. Macromol. 13, 14-16.
    • (1991) Int. J. Biol. Macromol. , vol.13 , pp. 14-16
    • Conway, J.F.1    Parry, D.A.D.2
  • 13
    • 0029083811 scopus 로고
    • Predicting oligomerization states of coiled coils
    • Woolfson, D.N. & Alber, T. (1995). Predicting oligomerization states of coiled coils. Protein Sci. 4, 1596-1607.
    • (1995) Protein Sci. , vol.4 , pp. 1596-1607
    • Woolfson, D.N.1    Alber, T.2
  • 14
    • 0024384644 scopus 로고
    • Preferential heterodimer formation by isolated leucine zippers from fos and jun
    • O'Shea, E.K., Rutkowski, R., Stafford, W.F., III & Kim, P.S. (1989). Preferential heterodimer formation by isolated leucine zippers from fos and jun. Science 245, 646-648.
    • (1989) Science , vol.245 , pp. 646-648
    • O'Shea, E.K.1    Rutkowski, R.2    Stafford III, W.F.3    Kim, P.S.4
  • 15
    • 0026571898 scopus 로고
    • Mechanism of specificity in the fos-jun oncoprotein heterodimer
    • O'Shea, E.K., Rutkowski, R. & Kim, P.S. (1992). Mechanism of specificity in the fos-jun oncoprotein heterodimer. Cell 68, 699-708.
    • (1992) Cell , vol.68 , pp. 699-708
    • O'Shea, E.K.1    Rutkowski, R.2    Kim, P.S.3
  • 16
    • 0027176792 scopus 로고
    • Dimerization specificity of the leucine-zipper-containing bZIP motif in DNA binding - Prediction and rational design
    • Vinson, C.R., Hai, J.W. & Boyd, S.M. (1993). Dimerization specificity of the leucine-zipper-containing bZIP motif in DNA binding - prediction and rational design. Genes Dev. 7, 1047-1058.
    • (1993) Genes Dev. , vol.7 , pp. 1047-1058
    • Vinson, C.R.1    Hai, J.W.2    Boyd, S.M.3
  • 17
    • 0000236570 scopus 로고
    • Peptide 'Velcro': Design of a heterodimeric coiled coil
    • O'Shea, E.K., Lumb, K.J. & Kim, P.S. (1993). Peptide 'Velcro': design of a heterodimeric coiled coil. Curr. Biol. 3, 658-667.
    • (1993) Curr. Biol. , vol.3 , pp. 658-667
    • O'Shea, E.K.1    Lumb, K.J.2    Kim, P.S.3
  • 19
    • 0021103673 scopus 로고
    • Periodic features in the amino acid sequence of nematode myosin rod
    • McLachlan, A.D. & Karn, J. (1983). Periodic features in the amino acid sequence of nematode myosin rod. J. Mol. Biol. 164, 605-626.
    • (1983) J. Mol. Biol. , vol.164 , pp. 605-626
    • McLachlan, A.D.1    Karn, J.2
  • 20
    • 0025601653 scopus 로고
    • Skip residues correlate with bends in the myosin tail
    • Offer, G. (1990). Skip residues correlate with bends in the myosin tail. J. Mol. Biol. 216, 213-218.
    • (1990) J. Mol. Biol. , vol.216 , pp. 213-218
    • Offer, G.1
  • 21
    • 0024279637 scopus 로고
    • Segmented α-helical coiled-coil structure of the protein giardin from the Giardia cytoskeleton
    • Holberton, D., Baker, D.A. & Marshall, J. (1988). Segmented α-helical coiled-coil structure of the protein giardin from the Giardia cytoskeleton. J. Mol. Biol. 204, 789-795.
    • (1988) J. Mol. Biol. , vol.204 , pp. 789-795
    • Holberton, D.1    Baker, D.A.2    Marshall, J.3
  • 22
    • 0027157011 scopus 로고
    • Sequence and structure of a new coiled-coil protein from a microtubule bundle in Giardia
    • Marshall, J. & Holberton, D.V. (1993). Sequence and structure of a new coiled-coil protein from a microtubule bundle in Giardia. J. Mol. Biol. 231, 521-530.
    • (1993) J. Mol. Biol. , vol.231 , pp. 521-530
    • Marshall, J.1    Holberton, D.V.2
  • 23
    • 0029099085 scopus 로고
    • Giardia gene predicts a 183 kDa nucleotide-binding head-stalk protein
    • Marshall, J. & Holberton, D.V. (1995). Giardia gene predicts a 183 kDa nucleotide-binding head-stalk protein. J. Cell Sci. 108, 2683-2692.
    • (1995) J. Cell Sci. , vol.108 , pp. 2683-2692
    • Marshall, J.1    Holberton, D.V.2
  • 24
    • 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
  • 26
    • 0027298784 scopus 로고
    • Aromatic side-chain contributions to far-ultraviolet circular dichroism of helical peptides and its effect an measurements of helix propensity
    • Chakrabartty, A., Kortemme, T., Padmanabhan, S. & Baldwin, R.L. (1993). Aromatic side-chain contributions to far-ultraviolet circular dichroism of helical peptides and its effect an measurements of helix propensity. Biochemistry 32, 5560-5565.
    • (1993) Biochemistry , vol.32 , pp. 5560-5565
    • Chakrabartty, A.1    Kortemme, T.2    Padmanabhan, S.3    Baldwin, R.L.4
  • 27
  • 28
    • 0028174643 scopus 로고
    • Quantitative determination of helical propensities from trifluoroethanol titration curves
    • Jasanoff, A. & Fersht, A.R. (1994). Quantitative determination of helical propensities from trifluoroethanol titration curves. Biochemistry 33, 2129-2135.
    • (1994) Biochemistry , vol.33 , pp. 2129-2135
    • Jasanoff, A.1    Fersht, A.R.2
  • 29
    • 0025849701 scopus 로고
    • Calorimetric determination of the enthalpy change for the α-helix to coil transition of an alanine peptide in water
    • [Published erratum appears in Proc. Natl. Acad. Sci. USA 1991 88, 6898]
    • Scholtz, J.M., et al., & Bolen, D.W. (1991). Calorimetric determination of the enthalpy change for the α-helix to coil transition of an alanine peptide in water. Proc. Natl. Acad. Sci. USA 88, 2854-2858. [Published erratum appears in Proc. Natl. Acad. Sci. USA 1991 88, 6898.]
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2854-2858
    • Scholtz, J.M.1    Bolen, D.W.2
  • 30
    • 0026679847 scopus 로고
    • Absence of the thermal transition in apo-α-lactalbumin in the molten globule state. a study by differential scanning microcalorimetry
    • Yutani, K., Ogasahara, K. & Kuwajima, K. (1992). Absence of the thermal transition in apo-α-lactalbumin in the molten globule state. A study by differential scanning microcalorimetry. J. Mol. Biol. 228, 347-350.
    • (1992) J. Mol. Biol. , vol.228 , pp. 347-350
    • Yutani, K.1    Ogasahara, K.2    Kuwajima, K.3
  • 31
    • 79954515341 scopus 로고
    • A de novo designed protein shows a thermally induced transition from a native to a molten globule-like state
    • Raleigh, D.P. & DeGrado, W.F. (1992). A de novo designed protein shows a thermally induced transition from a native to a molten globule-like state. J. Am. Chem. Soc. 114, 10079-10081.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10079-10081
    • Raleigh, D.P.1    DeGrado, W.F.2
  • 32
    • 0029942482 scopus 로고    scopus 로고
    • Hyperthermostable surface-layer protein tetrabrachion from the archaebacterium Staphylothermus marinus - Evidence for the presence of a right-handed coiled-coil derived from the primary structure
    • Peters, J., Baumeister, W. & Lupas, A. (1996). Hyperthermostable surface-layer protein tetrabrachion from the archaebacterium Staphylothermus marinus - evidence for the presence of a right-handed coiled-coil derived from the primary structure. J. Mol. Biol. 257, 1031-1041.
    • (1996) J. Mol. Biol. , vol.257 , pp. 1031-1041
    • Peters, J.1    Baumeister, W.2    Lupas, A.3
  • 33
    • 0000619593 scopus 로고    scopus 로고
    • A novel 11-residue coiled-coil motif predicts a histidine zipper
    • Werner, E., Holder, A.A., Aszodi, A. & Taylor, W.R. (1996). A novel 11-residue coiled-coil motif predicts a histidine zipper. Protein Pept. Lett. 3, 139-145.
    • (1996) Protein Pept. Lett. , vol.3 , pp. 139-145
    • Werner, E.1    Holder, A.A.2    Aszodi, A.3    Taylor, W.R.4
  • 34
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough, P.A., Hughson, F.M., Skehel, J.J. & 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
  • 35
    • 0027564435 scopus 로고
    • A repeating 11-mer amino-acid motif and plant desiccation
    • Dure, L.I. (1993). A repeating 11-mer amino-acid motif and plant desiccation. Plant J. 3, 363-369.
    • (1993) Plant J. , vol.3 , pp. 363-369
    • Dure, L.I.1
  • 36
    • 0029929966 scopus 로고    scopus 로고
    • A natural variant of type-l antifreeze protein with four icebinding repeats is a particularly potent antifreeze
    • Chao, H., Hodges, R.S., Kay, C.M., Gauthier, S.Y. & Davies, P.L. (1996). A natural variant of type-l antifreeze protein with four icebinding repeats is a particularly potent antifreeze. Protein Sci. 5, 1150-1156.
    • (1996) Protein Sci. , vol.5 , pp. 1150-1156
    • Chao, H.1    Hodges, R.S.2    Kay, C.M.3    Gauthier, S.Y.4    Davies, P.L.5
  • 38
    • 0027167511 scopus 로고
    • SF-assemblin, the structural protein of the 2-nm filaments from striated microtubule-associated fibers of algal flagellar roots, forms a segmented coiled coil
    • Weber, K., Geisler, N., Plessmann, U., Bremerich, A., Lechtreck, K.F. & Melkonian, M. (1993). SF-assemblin, the structural protein of the 2-nm filaments from striated microtubule-associated fibers of algal flagellar roots, forms a segmented coiled coil. J. Cell Biol. 121, 837-845.
    • (1993) J. Cell Biol. , vol.121 , pp. 837-845
    • Weber, K.1    Geisler, N.2    Plessmann, U.3    Bremerich, A.4    Lechtreck, K.F.5    Melkonian, M.6
  • 39
    • 0029863530 scopus 로고    scopus 로고
    • The cruciated microtubule-associated fibers of the green-alga Dunaliella bioculata consist of a 31-kDa SF-assemblin
    • Lechtreck, K.F., Frins, S., Bilski, J., Teltenkotter, A., Weber, K. & Melkonian, M. (1996). The cruciated microtubule-associated fibers of the green-alga Dunaliella bioculata consist of a 31-kDa SF-assemblin. J. Cell Sci. 109, 827-835.
    • (1996) J. Cell Sci. , vol.109 , pp. 827-835
    • Lechtreck, K.F.1    Frins, S.2    Bilski, J.3    Teltenkotter, A.4    Weber, K.5    Melkonian, M.6
  • 40
    • 0027532105 scopus 로고
    • Pitch diversity in α-helical coiled coils
    • Seo, J. & Cohen, C. (1993). Pitch diversity in α-helical coiled coils. Proteins 15, 223-234.
    • (1993) Proteins , vol.15 , pp. 223-234
    • Seo, J.1    Cohen, C.2
  • 41
    • 16944366990 scopus 로고    scopus 로고
    • Buried polar residues and structural specificity in the GCN4 leucine zipper
    • Gonzalez, L.J., Woolfson, D.N. & Alber, T. (1996). Buried polar residues and structural specificity in the GCN4 leucine zipper. Nat. Struct. Biol. 3, 1011-1018.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 1011-1018
    • Gonzalez, L.J.1    Woolfson, D.N.2    Alber, T.3
  • 42
    • 0027452754 scopus 로고
    • Regulation of heat shock factor trimer formation: Role of a conserved leucine zipper
    • Rabindran, S.K., Haroun, R.I., Clos, J., Wisniewski, J. & Wu, C. (1993). Regulation of heat shock factor trimer formation: role of a conserved leucine zipper. Science 259, 230-234.
    • (1993) Science , vol.259 , pp. 230-234
    • Rabindran, S.K.1    Haroun, R.I.2    Clos, J.3    Wisniewski, J.4    Wu, C.5
  • 43
    • 0029974730 scopus 로고    scopus 로고
    • An engineered allosteric switch in leucine-zipper oligomerization
    • Gonzalez, L., Plecs, J.J. & Alber, T. (1996). An engineered allosteric switch in leucine-zipper oligomerization. Nat. Struct. Biol. 3, 510-515.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 510-515
    • Gonzalez, L.1    Plecs, J.J.2    Alber, T.3
  • 44
    • 16944363590 scopus 로고    scopus 로고
    • Crystal structures of a single coiled-coil peptide in two oligomeric states reveal the basis for structural polymorphism
    • Gonzalez, L.J., Brown, R.A., Richardson, D. & Alber, T. (1996). Crystal structures of a single coiled-coil peptide in two oligomeric states reveal the basis for structural polymorphism. Nat. Struct. Biol. 3, 1002-1010.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 1002-1010
    • Gonzalez, L.J.1    Brown, R.A.2    Richardson, D.3    Alber, T.4
  • 45
    • 0025272940 scopus 로고
    • α-Helical coiled coils and bundles - How to design an α-helical protein
    • Cohen, C. & Parry, D.A.D. (1990). α-Helical coiled coils and bundles - how to design an α-helical protein. Proteins 7, 1-15.
    • (1990) Proteins , vol.7 , pp. 1-15
    • Cohen, C.1    Parry, D.A.D.2
  • 46
    • 0028987628 scopus 로고
    • Model structure of the omp-α rod, a parallel four-stranded coiled coil from the hyperthermophilic eubacterium Thermotoga maritima
    • Lupas, A., Muller, S., Goldie, K., Engel, A.M., Engel, A. & Baumeister, W. (1995). Model structure of the omp-α rod, a parallel four-stranded coiled coil from the hyperthermophilic eubacterium Thermotoga maritima. J. Mol. Biol. 248, 180-189.
    • (1995) J. Mol. Biol. , vol.248 , pp. 180-189
    • Lupas, A.1    Muller, S.2    Goldie, K.3    Engel, A.M.4    Engel, A.5    Baumeister, W.6
  • 47
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino-acid-sequence data
    • Gill, S.C. & Von Hippel, P.H. (1939). Calculation of protein extinction coefficients from amino-acid-sequence data. Analyt. Biochem. 182, 319-326.
    • (1939) Analyt. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 48
    • 0026244229 scopus 로고
    • MOLSCRIPT - A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT - a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


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