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Volumn 186, Issue 3, 2014, Pages 402-411

Convergently-evolved structural anomalies in the coiled coil domains of insect silk proteins

Author keywords

Cocoons; Coiled coil; Helices; Insect; Protein; Silk

Indexed keywords

ALANINE; INSECT PROTEIN; INSECT SILK PROTEIN; INTRINSICALLY DISORDERED PROTEIN; LEUCINE ZIPPER PROTEIN; TROPOMYOSIN; UNCLASSIFIED DRUG; SILK;

EID: 84901623481     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2014.01.002     Document Type: Article
Times cited : (21)

References (69)
  • 1
    • 0027297241 scopus 로고
    • Genetic analysis of the leucine heptad repeats of Lac repressor: evidence for a 4-helical bundle
    • Alberti S., Oehler S., von Wilcken-Bergmann B., Müller-Hill B. Genetic analysis of the leucine heptad repeats of Lac repressor: evidence for a 4-helical bundle. EMBO J. 1993, 12:3227-3236.
    • (1993) EMBO J. , vol.12 , pp. 3227-3236
    • Alberti, S.1    Oehler, S.2    von Wilcken-Bergmann, B.3    Müller-Hill, B.4
  • 2
    • 0342775633 scopus 로고
    • A four-strand coiled coil model for some insect fibrous proteins
    • Atkins E.D.T. A four-strand coiled coil model for some insect fibrous proteins. J. Mol. Biol. 1967, 24:139-140.
    • (1967) J. Mol. Biol. , vol.24 , pp. 139-140
    • Atkins, E.D.T.1
  • 6
    • 0007912642 scopus 로고
    • Observations on the mechanism of a tanning reaction in Periplaneta and Blatta
    • Brunet P.C.J., Kent P.W. Observations on the mechanism of a tanning reaction in Periplaneta and Blatta. Proc. R. Soc. London B 1955, 144:259-274.
    • (1955) Proc. R. Soc. London B , vol.144 , pp. 259-274
    • Brunet, P.C.J.1    Kent, P.W.2
  • 7
    • 0025146205 scopus 로고
    • High-resolution spot-scan electron microscopy of microcrystals of an alpha-helical coiled-coil protein
    • Bullough P.A., Tulloch P.A. High-resolution spot-scan electron microscopy of microcrystals of an alpha-helical coiled-coil protein. J. Mol. Biol. 1990, 215:161-173.
    • (1990) J. Mol. Biol. , vol.215 , pp. 161-173
    • Bullough, P.A.1    Tulloch, P.A.2
  • 10
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence
    • Chou P.Y., Fasman G.D. Prediction of the secondary structure of proteins from their amino acid sequence. Adv. Enzymol. Relat. Areas Mol. Biol. 1978, 47:45-148.
    • (1978) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2
  • 11
    • 34250268094 scopus 로고
    • Oecophylla silk - functional adaptation in a biopolymer
    • Crewe R.M., Thompson P.R. Oecophylla silk - functional adaptation in a biopolymer. Naturwissenschaften 1979, 66:57-58.
    • (1979) Naturwissenschaften , vol.66 , pp. 57-58
    • Crewe, R.M.1    Thompson, P.R.2
  • 12
    • 0001105482 scopus 로고
    • Is α-keratin a coiled coil?
    • Crick F.H.C. Is α-keratin a coiled coil?. Nature 1952, 170:882-883.
    • (1952) Nature , vol.170 , pp. 882-883
    • Crick, F.H.C.1
  • 13
    • 0000920828 scopus 로고
    • The packing of α-helices: simple coiled-coils
    • Crick F.H.C. The packing of α-helices: simple coiled-coils. Acta Crystallogr. 1953, 6:689-697.
    • (1953) Acta Crystallogr. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 14
    • 0035999986 scopus 로고    scopus 로고
    • An HMM model for coiled-coil domains and a comparison with PSSM-based predictions
    • Delorenzi M., Speed T. An HMM model for coiled-coil domains and a comparison with PSSM-based predictions. Bioinformatics 2002, 18:617-625.
    • (2002) Bioinformatics , vol.18 , pp. 617-625
    • Delorenzi, M.1    Speed, T.2
  • 15
    • 32044459935 scopus 로고    scopus 로고
    • Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat
    • Deng Y., Liu J., Zheng Q., Eliezer D., Kallenbach N.R., Lu M. Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat. Structure 2006, 14:247-255.
    • (2006) Structure , vol.14 , pp. 247-255
    • Deng, Y.1    Liu, J.2    Zheng, Q.3    Eliezer, D.4    Kallenbach, N.R.5    Lu, M.6
  • 16
    • 77951974524 scopus 로고    scopus 로고
    • Measuring the conformational space of square four-helical bundles with the program samCC
    • Dunin-Horkawicz S., Lupas A.N. Measuring the conformational space of square four-helical bundles with the program samCC. J. Struct. Biol. 2010, 170:226-235.
    • (2010) J. Struct. Biol. , vol.170 , pp. 226-235
    • Dunin-Horkawicz, S.1    Lupas, A.N.2
  • 17
    • 84964165967 scopus 로고
    • A two-phase structure for keratin fibers
    • Feughelman M. A two-phase structure for keratin fibers. Text. Res. J. 1959, 29:223-228.
    • (1959) Text. Res. J. , vol.29 , pp. 223-228
    • Feughelman, M.1
  • 18
    • 0014052711 scopus 로고
    • Sudies on insect fibrous proteins: the larval silk of Apis, Bombus and Vespa (Hymenoptera: Aculeata)
    • Flower N.E., Kenchington W. Sudies on insect fibrous proteins: the larval silk of Apis, Bombus and Vespa (Hymenoptera: Aculeata). J. R. Microsc. Soc. 1967, 86:297-310.
    • (1967) J. R. Microsc. Soc. , vol.86 , pp. 297-310
    • Flower, N.E.1    Kenchington, W.2
  • 20
    • 0003100933 scopus 로고
    • Raman spectroscopy of proteins
    • Heyden, New York, R.S.H. Clark, R.E. Hester (Eds.)
    • Frushour B.G., Koenig J.L. Raman spectroscopy of proteins. Advances in Infrared and Raman Spectroscopy 1975, 35-97. Heyden, New York. R.S.H. Clark, R.E. Hester (Eds.).
    • (1975) Advances in Infrared and Raman Spectroscopy , pp. 35-97
    • Frushour, B.G.1    Koenig, J.L.2
  • 22
    • 23144450570 scopus 로고    scopus 로고
    • REPPER - repeats and their periodicities in fibrous proteins
    • Gruber M., Söding J., Lupas A.N. REPPER - repeats and their periodicities in fibrous proteins. Nucl. Acids Res. 2005, 3:W239-W243.
    • (2005) Nucl. Acids Res. , vol.3
    • Gruber, M.1    Söding, J.2    Lupas, A.N.3
  • 24
    • 84871356128 scopus 로고    scopus 로고
    • Structural and physical changes of honeybee silk materials induced by heating or by immersion in aqueous methanol solutions
    • Huson M.G., Church J.S., Poole J.M., Weisman S., Sriskantha S., Warden A.C., Ramshaw J.A.M., Sutherland T.D. Structural and physical changes of honeybee silk materials induced by heating or by immersion in aqueous methanol solutions. PLoS One 2012, 7:e52308. 10.1371/journal.pone.0052308.
    • (2012) PLoS One , vol.7
    • Huson, M.G.1    Church, J.S.2    Poole, J.M.3    Weisman, S.4    Sriskantha, S.5    Warden, A.C.6    Ramshaw, J.A.M.7    Sutherland, T.D.8
  • 25
    • 1942473116 scopus 로고    scopus 로고
    • Shorter side chains optimize helix-helix packing. Shorter side chains optimize helix-helix packing
    • Jiang S., Vakser I.A. Shorter side chains optimize helix-helix packing. Shorter side chains optimize helix-helix packing. Protein Sci. 2004, 13:1426-1429.
    • (2004) Protein Sci. , vol.13 , pp. 1426-1429
    • Jiang, S.1    Vakser, I.A.2
  • 26
    • 0042364941 scopus 로고    scopus 로고
    • Mechanism of silk processing in insects and spiders
    • Jin H.J., Kaplan D.L. Mechanism of silk processing in insects and spiders. Nature 2003, 424:1057-1061.
    • (2003) Nature , vol.424 , pp. 1057-1061
    • Jin, H.J.1    Kaplan, D.L.2
  • 27
    • 84864690437 scopus 로고    scopus 로고
    • Quantifying the fraction of alanine residues in an-helical conformation in hornet silk using solid-state NMR
    • Kameda T. Quantifying the fraction of alanine residues in an-helical conformation in hornet silk using solid-state NMR. Polym. J. 2012, 44:876-881.
    • (2012) Polym. J. , vol.44 , pp. 876-881
    • Kameda, T.1
  • 28
    • 57849083635 scopus 로고    scopus 로고
    • 13C solid-state NMR study of the molecular structure of honeybee wax and silk
    • 13C solid-state NMR study of the molecular structure of honeybee wax and silk. Int. J. Biol. Macromol. 2009, 44:64-69.
    • (2009) Int. J. Biol. Macromol. , vol.44 , pp. 64-69
    • Kameda, T.1    Tamada, Y.2
  • 29
    • 29844436662 scopus 로고    scopus 로고
    • Film formation and structural characterization of silk of the hornet Vespa simillima xanthoptera Cameron
    • Kameda T., Kojima K., Miyazawa M., Fujiwara S. Film formation and structural characterization of silk of the hornet Vespa simillima xanthoptera Cameron. Z. Naturforsch., C: J. Biosci. 2005, 60:906-914.
    • (2005) Z. Naturforsch., C: J. Biosci. , vol.60 , pp. 906-914
    • Kameda, T.1    Kojima, K.2    Miyazawa, M.3    Fujiwara, S.4
  • 32
    • 0014449674 scopus 로고
    • Flower Studies on insect fibrous proteins: the structural protein of the ootheca in the praying mantis, Sphodromantis centralis Rehn
    • Kenchington W., Flower Studies on insect fibrous proteins: the structural protein of the ootheca in the praying mantis, Sphodromantis centralis Rehn. J. Microsc. 1967, 89:263-281.
    • (1967) J. Microsc. , vol.89 , pp. 263-281
    • Kenchington, W.1
  • 33
    • 0033531474 scopus 로고    scopus 로고
    • Liquid crystals and flow elongation in a spider's silk production line
    • Knight D.P., Vollrath F. Liquid crystals and flow elongation in a spider's silk production line. Proc. R. Soc. B 1999, 266:519-523.
    • (1999) Proc. R. Soc. B , vol.266 , pp. 519-523
    • Knight, D.P.1    Vollrath, F.2
  • 34
    • 2442655493 scopus 로고    scopus 로고
    • Stabilising and destabilizing clusters in the hydrophobic core of long two-stranded alpha helical coiled coils
    • Kwok S.C., Hodges R.S. Stabilising and destabilizing clusters in the hydrophobic core of long two-stranded alpha helical coiled coils. J. Biol. Chem. 2004, 279:576-588.
    • (2004) J. Biol. Chem. , vol.279 , pp. 576-588
    • Kwok, S.C.1    Hodges, R.S.2
  • 35
    • 73149102752 scopus 로고    scopus 로고
    • The shape and flexibility of tropomyosin coiled coils: implications for actin filament assembly and regulation
    • Li X.E., Holmes K.C., Lehman W., Jung H., Fischer S. The shape and flexibility of tropomyosin coiled coils: implications for actin filament assembly and regulation. J. Mol. Biol. 2010, 395:327-339.
    • (2010) J. Mol. Biol. , vol.395 , pp. 327-339
    • Li, X.E.1    Holmes, K.C.2    Lehman, W.3    Jung, H.4    Fischer, S.5
  • 36
    • 77951975707 scopus 로고    scopus 로고
    • Curvature variation along the Tropomysin molecule. Curvature variation along the tropomyosin molecule
    • Li X.E., Lehman W., Fischer S., Holmes K.C. Curvature variation along the Tropomysin molecule. Curvature variation along the tropomyosin molecule. J. Struct. Biol. 2010, 170:307-312.
    • (2010) J. Struct. Biol. , vol.170 , pp. 307-312
    • Li, X.E.1    Lehman, W.2    Fischer, S.3    Holmes, K.C.4
  • 37
    • 0037073681 scopus 로고    scopus 로고
    • An alanine-zipper structure determined by long-range intermolecular interactions
    • Liu J., Lu M. An alanine-zipper structure determined by long-range intermolecular interactions. J. Biol. Chem. 2002, 277:48708-48713.
    • (2002) J. Biol. Chem. , vol.277 , pp. 48708-48713
    • Liu, J.1    Lu, M.2
  • 38
    • 0001295683 scopus 로고
    • Extracellular fibrous proteins: the silks
    • Elsevier, Amsterdam
    • Lucas F., Rudall K.M. Extracellular fibrous proteins: the silks. Comprehensive Biochemistry 1968, vol. 26:475-558. Elsevier, Amsterdam.
    • (1968) Comprehensive Biochemistry , vol.26 , pp. 475-558
    • Lucas, F.1    Rudall, K.M.2
  • 39
    • 17444424974 scopus 로고    scopus 로고
    • The structure of alpha-helical coiled coils
    • Lupas A.N., Gruber M. The structure of alpha-helical coiled coils. Adv. Protein Chem. 2005, 70:37-78.
    • (2005) Adv. Protein Chem. , vol.70 , pp. 37-78
    • Lupas, A.N.1    Gruber, M.2
  • 40
    • 84971301149 scopus 로고
    • The effects of shape on the interaction of colloidal particles
    • Onsager L. The effects of shape on the interaction of colloidal particles. Ann. N.Y. Acad. Sci. 1949, 51:627-659.
    • (1949) Ann. N.Y. Acad. Sci. , vol.51 , pp. 627-659
    • Onsager, L.1
  • 42
    • 59249109225 scopus 로고    scopus 로고
    • Silk as a biomimetic ideal for structural polymers
    • Porter D., Vollrath F. Silk as a biomimetic ideal for structural polymers. Adv. Mater. 2009, 21:487-492.
    • (2009) Adv. Mater. , vol.21 , pp. 487-492
    • Porter, D.1    Vollrath, F.2
  • 43
    • 84874905314 scopus 로고    scopus 로고
    • Spider silk: super material or thin fibre?
    • Porter D., Guan J., Vollrath F. Spider silk: super material or thin fibre?. Adv. Mater. 2013, 25:1275-1279.
    • (2013) Adv. Mater. , vol.25 , pp. 1275-1279
    • Porter, D.1    Guan, J.2    Vollrath, F.3
  • 44
    • 4143077357 scopus 로고    scopus 로고
    • Helical shifts generate two distinct conformers in the atomic resolution structure of the CheA phosphotransferase domain from Thermotoga maritima
    • Quezada C.M., Gradinaru C., Simon M.I., Bilwes A.M., Crane B.R. Helical shifts generate two distinct conformers in the atomic resolution structure of the CheA phosphotransferase domain from Thermotoga maritima. J. Mol. Biol. 2004, 341:1283-1294.
    • (2004) J. Mol. Biol. , vol.341 , pp. 1283-1294
    • Quezada, C.M.1    Gradinaru, C.2    Simon, M.I.3    Bilwes, A.M.4    Crane, B.R.5
  • 45
    • 84901607101 scopus 로고
    • (Ph.D. thesis). University of Oxford.
    • Rattew, C.J., 1974. (Ph.D. thesis). University of Oxford.
    • (1974)
    • Rattew, C.J.1
  • 46
    • 0037481245 scopus 로고
    • Protein ribbons and sheets
    • Rudall K.M. Protein ribbons and sheets. Sci. Basis Med. 1956, 5:217-230.
    • (1956) Sci. Basis Med. , vol.5 , pp. 217-230
    • Rudall, K.M.1
  • 47
    • 0006365890 scopus 로고
    • Silk and other cocoon proteins
    • Academic Press, New York
    • Rudall K.M. Silk and other cocoon proteins. Comparative Biochemistry 1962, vol. IV:397-433. Academic Press, New York.
    • (1962) Comparative Biochemistry , vol.4 , pp. 397-433
    • Rudall, K.M.1
  • 48
    • 0002472233 scopus 로고
    • Arthropod silks: the problem of fibrous proteins in animal tissues
    • Rudall K.M., Kenchington W. Arthropod silks: the problem of fibrous proteins in animal tissues. Annu. Rev. Entomol. 1971, 16:73-96.
    • (1971) Annu. Rev. Entomol. , vol.16 , pp. 73-96
    • Rudall, K.M.1    Kenchington, W.2
  • 49
    • 36448956824 scopus 로고    scopus 로고
    • Identification of four major hornet silk genes with a complex of alanine-rich and serine-rich sequences in Vespa simillima xanthoptera Cameron
    • Sezutzu H., Kajiwara H., Kojima K., Mita K., Tamura T., Tamada Y., Kameda T. Identification of four major hornet silk genes with a complex of alanine-rich and serine-rich sequences in Vespa simillima xanthoptera Cameron. Biosci. Biotech. Biochem. 2007, 71:2725-2734.
    • (2007) Biosci. Biotech. Biochem. , vol.71 , pp. 2725-2734
    • Sezutzu, H.1    Kajiwara, H.2    Kojima, K.3    Mita, K.4    Tamura, T.5    Tamada, Y.6    Kameda, T.7
  • 50
    • 42049105554 scopus 로고    scopus 로고
    • Identification, recombinant production and structural characterization of four silk proteins from the Asiatic honeybee Apis cerana
    • Shi J., Lua S., Du N., Liu X., Song J. Identification, recombinant production and structural characterization of four silk proteins from the Asiatic honeybee Apis cerana. Biomaterials 2008, 29:2820-2828.
    • (2008) Biomaterials , vol.29 , pp. 2820-2828
    • Shi, J.1    Lua, S.2    Du, N.3    Liu, X.4    Song, J.5
  • 51
    • 0034674154 scopus 로고    scopus 로고
    • Core structure of the outer membrane lipoprotein from Escherichia coli at 1.9Å resolution
    • Shu W., Liu J., Ji H., Lu M. Core structure of the outer membrane lipoprotein from Escherichia coli at 1.9Å resolution. J. Mol. Biol. 2000, 299:1101-1112.
    • (2000) J. Mol. Biol. , vol.299 , pp. 1101-1112
    • Shu, W.1    Liu, J.2    Ji, H.3    Lu, M.4
  • 52
    • 0346874294 scopus 로고    scopus 로고
    • Silk formation mechanisms in the larval salivary glands of Apis mellifera (Hymenoptera: Apidae)
    • Silva-Zacarin E.C.M., Silva De Moraes R.L.M., Taboga S.R. Silk formation mechanisms in the larval salivary glands of Apis mellifera (Hymenoptera: Apidae). J. Biosci. 2003, 28:753-764.
    • (2003) J. Biosci. , vol.28 , pp. 753-764
    • Silva-Zacarin, E.C.M.1    Silva De Moraes, R.L.M.2    Taboga, S.R.3
  • 53
    • 0344198181 scopus 로고    scopus 로고
    • Local destabilization of the tropomyosin coiled coil gives the molecular flexibility required for actin binding
    • Singh A., Hitchcock-DeGregori S.E. Local destabilization of the tropomyosin coiled coil gives the molecular flexibility required for actin binding. Biochemistry 2003, 42:14114-14121.
    • (2003) Biochemistry , vol.42 , pp. 14114-14121
    • Singh, A.1    Hitchcock-DeGregori, S.E.2
  • 59
    • 84871757783 scopus 로고    scopus 로고
    • LOGICOIL-multistate prediction of coiled coil oligomeric state
    • Vincent T.L., Green P.L., Woolfson D.N. LOGICOIL-multistate prediction of coiled coil oligomeric state. Bioinformatics 2013, 29:69-76.
    • (2013) Bioinformatics , vol.29 , pp. 69-76
    • Vincent, T.L.1    Green, P.L.2    Woolfson, D.N.3
  • 60
    • 84870901451 scopus 로고    scopus 로고
    • Natural templates for coiled coil biomaterials from praying mantis egg-cases
    • Walker A.A., Weisman S., Kameda T., Sutherland T.D. Natural templates for coiled coil biomaterials from praying mantis egg-cases. Biomacromolecules 2012, 13:4264-4272.
    • (2012) Biomacromolecules , vol.13 , pp. 4264-4272
    • Walker, A.A.1    Weisman, S.2    Kameda, T.3    Sutherland, T.D.4
  • 62
    • 0029867179 scopus 로고    scopus 로고
    • Principles of helix-helix packing in proteins: the helical lattice superposition model
    • Walther D., Eisenhaber F., Argos P. Principles of helix-helix packing in proteins: the helical lattice superposition model. J. Mol. Biol. 1996, 255:536-553.
    • (1996) J. Mol. Biol. , vol.255 , pp. 536-553
    • Walther, D.1    Eisenhaber, F.2    Argos, P.3
  • 67
    • 17444433002 scopus 로고    scopus 로고
    • The design of coiled coil structures and assemblies
    • San Diego Elsevier, CA, D.A.D. Parry, J.M. Squire (Eds.)
    • Woolfson D.N. The design of coiled coil structures and assemblies. Fibrous Proteins: Coiled-Coils, Collagen and Elastomers 2005, 79-112. San Diego Elsevier, CA. D.A.D. Parry, J.M. Squire (Eds.).
    • (2005) Fibrous Proteins: Coiled-Coils, Collagen and Elastomers , pp. 79-112
    • Woolfson, D.N.1
  • 68
    • 48749138307 scopus 로고
    • The identification of N-acyldopamine glucosides in the left colleterial gland of the praying mantids Mantis religiosa L., Statilia maculata Thunberg, and Tenodera augustipennis Saussure
    • Yago M., Hitoshi S., Kawasaki H. The identification of N-acyldopamine glucosides in the left colleterial gland of the praying mantids Mantis religiosa L., Statilia maculata Thunberg, and Tenodera augustipennis Saussure. Insect Biochem. 1984, 14:7-9.
    • (1984) Insect Biochem. , vol.14 , pp. 7-9
    • Yago, M.1    Hitoshi, S.2    Kawasaki, H.3
  • 69
    • 45149138747 scopus 로고
    • Enzymatic activities involved in the oothecal sclerotization of the praying mantid, Tenodera arififolia sinensis Saussure
    • Yago M., Hitoshi S., Oshima S., Hiroya K. Enzymatic activities involved in the oothecal sclerotization of the praying mantid, Tenodera arififolia sinensis Saussure. Insect Biochem. 1990, 20:745-750.
    • (1990) Insect Biochem. , vol.20 , pp. 745-750
    • Yago, M.1    Hitoshi, S.2    Oshima, S.3    Hiroya, K.4


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