메뉴 건너뛰기




Volumn 19, Issue 7, 2010, Pages 1366-1375

How sequence directs bending in tropomyosin and other two-stranded alpha-helical coiled coils

Author keywords

Alpha helical coiled coil; Axial stagger; Bends; Gaps; Joints; Regulation of muscle contraction; Semi flexibility; Tropomyosin

Indexed keywords

F ACTIN; MYOSIN; TROPOMYOSIN;

EID: 77954003079     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.415     Document Type: Article
Times cited : (21)

References (43)
  • 1
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • O'Shea EK, Klemm JD, Kim PS, 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
  • 2
    • 0035252931 scopus 로고    scopus 로고
    • Coiled coils: A highly versatile protein folding motif
    • DOI 10.1016/S0962-8924(00)01898-5, PII S0962892400018985
    • Burkhard P, Stetefeld J, Strelkov SV (2001) Coiled coils: a highly versatile protein folding motif. Trends Cell Biol 11:82-88. (Pubitemid 32144755)
    • (2001) Trends in Cell Biology , vol.11 , Issue.2 , pp. 82-88
    • Burkhard, P.1    Stetefeld, J.2    Strelkov, S.V.3
  • 3
    • 26844510875 scopus 로고    scopus 로고
    • Regulation of muscle contraction by tropomyosin and troponin: How structure illuminates function
    • Squire JM, Parry DA, Eds. Elsevier/Academic press
    • Brown JH, Cohen C, Regulation of muscle contraction by tropomyosin and troponin: how structure illuminates function. In: Squire JM, Parry DA, Eds. (2005) Fibrous proteins and related structures. Elsevier/Academic press.
    • (2005) Fibrous Proteins and Related Structures
    • Brown, J.H.1    Cohen, C.2
  • 4
    • 0000920828 scopus 로고
    • The packing of alpha-helices: Simple coiled coils
    • Crick FHC (1953) The packing of alpha-helices: simple coiled coils. Acta Crystallogr 6:689-697.
    • (1953) Acta Crystallogr , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 5
    • 0025272940 scopus 로고
    • Alpha-helical coiled coils and bundles: How to design an alpha-helical protein
    • Cohen C, Parry DAD (1990) Alpha-helical coiled coils and bundles: how to design an alpha-helical protein. Protein Struct Funct Genet 7:1-15.
    • (1990) Protein Struct Funct Genet , vol.7 , pp. 1-15
    • Cohen, C.1    Parry, D.A.D.2
  • 6
    • 0035853291 scopus 로고    scopus 로고
    • SOCKET: A program for identifying and analysing coiled-coil motifs within protein structures
    • DOI 10.1006/jmbi.2001.4545
    • Walshaw J, Woolfson DN (2001) Socket: a program for identifying and analyzing coiled-coil motifs within protein structures. J Mol Biol 307:1427-1450. (Pubitemid 33027651)
    • (2001) Journal of Molecular Biology , vol.307 , Issue.5 , pp. 1427-1450
    • Walshaw, J.1    Woolfson, D.N.2
  • 8
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin AG, Brenner SE, Hubbard T, Chothia C (1995) SCOP: a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 247:536-540.
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 9
    • 0020446736 scopus 로고
    • Coiled-coils in alpha-helix-containing proteins: Analysis of the residue types within the heptad repeat and the use of these data in the prediction of coiled-coils in other proteins
    • Parry DA (1982) Coiled-coils in alpha-helix-containing proteins: analysis of the residue types within the heptad repeat and the use of these data in the prediction of coiled-coils in other proteins. Biosci Rep 2: 1017-1024.
    • (1982) Biosci Rep , vol.2 , pp. 1017-1024
    • Parry, D.A.1
  • 11
    • 33747788700 scopus 로고    scopus 로고
    • Comparative analysis of coiled-coil prediction methods
    • DOI 10.1016/j.jsb.2006.03.009, PII S1047847706000815, Fibrous Protein Structure
    • Gruber M, Soding J, Lupas AN (2006) Comparative analysis of coiled-coil prediction methods. J Struct Biol 155:140-145. (Pubitemid 44278640)
    • (2006) Journal of Structural Biology , vol.155 , Issue.2 , pp. 140-145
    • Gruber, M.1    Soding, J.2    Lupas, A.N.3
  • 12
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas A, Van Dyke M, Stock J (1991) Predicting coiled coils from protein sequences. Science 252:1162-1164. (Pubitemid 21917026)
    • (1991) Science , vol.252 , Issue.5009 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 13
    • 17444433002 scopus 로고    scopus 로고
    • The design of coiled-coil structures and assemblies
    • Woolfson DN (2005) The design of coiled-coil structures and assemblies. Adv Protein Chem 70:79-112.
    • (2005) Adv Protein Chem , vol.70 , pp. 79-112
    • Woolfson, D.N.1
  • 14
    • 17444424974 scopus 로고    scopus 로고
    • The structure of alpha-helical coiled coils
    • Lupas AN, Gruber M (2005) The structure of alpha-helical coiled coils. Adv Protein Chem 70:37-78.
    • (2005) Adv Protein Chem , vol.70 , pp. 37-78
    • Lupas, A.N.1    Gruber, M.2
  • 15
    • 0036445512 scopus 로고    scopus 로고
    • Analysis of alpha-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation
    • Strelkov SV, Burkhard P (2002) Analysis of alpha-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation. J Struct Biol 137:54-64.
    • (2002) J Struct Biol , vol.137 , pp. 54-64
    • Strelkov, S.V.1    Burkhard, P.2
  • 16
    • 0035902460 scopus 로고    scopus 로고
    • Structural basis for bending tropomyosin around actin in muscle thin filaments
    • Stewart M (2001) Structural basis for bending tropomyosin around actin in muscle thin filaments. Proc Natl Acad Sci USA 98:8165-8166.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 8165-8166
    • Stewart, M.1
  • 18
    • 29344461522 scopus 로고    scopus 로고
    • Breaking symmetry in protein dimers: Designs and functions
    • Brown JH (2006) Breaking symmetry in protein dimers: designs and functions. Protein Sci 15:1-13.
    • (2006) Protein Sci , vol.15 , pp. 1-13
    • Brown, J.H.1
  • 21
    • 47749129993 scopus 로고    scopus 로고
    • Two-crystal structures of tropomyosin C-terminal fragment 176-273: Exposure of the hydrophobic core to the solvent destabilizes the tropomyosin molecule
    • Minakata S, Maeda K, Oda N, Wakabayashi K, Nitanai Y, Maeda Y (2008) Two-crystal structures of tropomyosin C-terminal fragment 176-273: exposure of the hydrophobic core to the solvent destabilizes the tropomyosin molecule. Biophys J 95:710-719.
    • (2008) Biophys J , vol.95 , pp. 710-719
    • Minakata, S.1    Maeda, K.2    Oda, N.3    Wakabayashi, K.4    Nitanai, Y.5    Maeda, Y.6
  • 22
    • 62449145371 scopus 로고    scopus 로고
    • Gestalt-binding of tropomyosin to actin filaments
    • Holmes KC, Lehman W (2008) Gestalt-binding of tropomyosin to actin filaments. J Muscle Res Cell Motil 29: 213-219.
    • (2008) J Muscle Res Cell Motil , vol.29 , pp. 213-219
    • Holmes, K.C.1    Lehman, W.2
  • 23
    • 33644795360 scopus 로고    scopus 로고
    • Dual requirement for flexibility and specificity for binding of the coiled-coil tropomyosin to its target, actin
    • Singh A, Hitchcock-DeGregori SE (2006) Dual requirement for flexibility and specificity for binding of the coiled-coil tropomyosin to its target, actin. Structure 14:43-50.
    • (2006) Structure , vol.14 , pp. 43-50
    • Singh, A.1    Hitchcock-DeGregori, S.E.2
  • 24
    • 77949474779 scopus 로고    scopus 로고
    • Proteomimicry: Simple engineering principles can be derived from the structures of proteins
    • Brown JH (2009) Proteomimicry: simple engineering principles can be derived from the structures of proteins. Am Sci 97:317-325.
    • (2009) Am Sci , vol.97 , pp. 317-325
    • Brown, J.H.1
  • 25
    • 0029867179 scopus 로고    scopus 로고
    • Principles of helix-helix packing in proteins: The helical lattice superposition model
    • Walther D, Eisenhaber F, Argos P (1996) Principles of helix-helix packing in proteins: the helical lattice superposition model. J Mol Biol 255:536-553.
    • (1996) J Mol Biol , vol.255 , pp. 536-553
    • Walther, D.1    Eisenhaber, F.2    Argos, P.3
  • 28
    • 59549088662 scopus 로고    scopus 로고
    • ProtorP: A protein- Protein interaction analysis server
    • Reynolds C, Damerell D, Jones S (2009) ProtorP: a protein- protein interaction analysis server. Bioinformatics 25:413-414.
    • (2009) Bioinformatics , vol.25 , pp. 413-414
    • Reynolds, C.1    Damerell, D.2    Jones, S.3
  • 29
    • 0042808434 scopus 로고    scopus 로고
    • Visualization of an unstable coiled coil from the scallop myosin rod
    • DOI 10.1038/nature01801
    • Li Y, Brown JH, Reshetnikova L, Blazsek A, Farkas L, Nyitray L, Cohen C (2003) Visualization of an unstable coiled coil from the scallop myosin rod. Nature 424: 341-345. (Pubitemid 36899379)
    • (2003) Nature , vol.424 , Issue.6946 , pp. 341-345
    • Li, Y.1    Brown, J.H.2    Reshetnikova, L.3    Blazsek, A.4    Farkas, L.5    Nyitray, L.6    Cohen, C.7
  • 30
    • 73149102752 scopus 로고    scopus 로고
    • The shape and flexibility of tropomyosin coiled coils: Implications for actin filament assembly and regulation
    • Li XE, Holmes KC, Lehman W, Jung H, Fischer S (2010) The shape and flexibility of tropomyosin coiled coils: implications for actin filament assembly and regulation. J Mol Biol 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
  • 31
    • 0344198181 scopus 로고    scopus 로고
    • Local Destabilization of the Tropomyosin Coiled Coil Gives the Molecular Flexibility Required for Actin Binding
    • DOI 10.1021/bi0348462
    • Singh A, Hitchcock-DeGregori SE (2003) Local destabilization of the tropomyosin coiled coil gives the molecular flexibility required for actin binding. Biochemistry 42:14114-14121. (Pubitemid 37499407)
    • (2003) Biochemistry , vol.42 , Issue.48 , pp. 14114-14121
    • Singh, A.1    Hitchcock-DeGregori, S.E.2
  • 32
    • 0016777712 scopus 로고
    • Analysis of the primary sequence of alpha-tropomyosin from rabbit skeletal muscle
    • Parry DA (1975) Analysis of the primary sequence of alpha-tropomyosin from rabbit skeletal muscle. J Mol Biol 98:519-535.
    • (1975) J Mol Biol , vol.98 , pp. 519-535
    • Parry, D.A.1
  • 33
    • 0017136639 scopus 로고
    • The 14-fold periodicity in alpha-tropomyosin and the interaction with actin
    • McLachlan AD, Stewart M (1976) The 14-fold periodicity in alpha-tropomyosin and the interaction with actin. J Mol Biol 103:271-298.
    • (1976) J Mol Biol , vol.103 , pp. 271-298
    • McLachlan, A.D.1    Stewart, M.2
  • 34
    • 0023042847 scopus 로고
    • Tropomyosin crystal structure and muscle regulation
    • Phillips GN, Fillers JP, Cohen C (1986) Tropomyosin crystal structure and muscle regulation. J Mol Biol 192:111-131.
    • (1986) J Mol Biol , vol.192 , pp. 111-131
    • Phillips, G.N.1    Fillers, J.P.2    Cohen, C.3
  • 35
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament
    • McKillop DFA, Geeves MA (1993) Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. Biophys J 65:693-701.
    • (1993) Biophys J , vol.65 , pp. 693-701
    • McKillop, D.F.A.1    Geeves, M.A.2
  • 36
    • 0031566964 scopus 로고    scopus 로고
    • Steric-model for activation of muscle thin filaments
    • DOI 10.1006/jmbi.1996.0800
    • Vibert P, Craig R, Lehman W (1997) Steric-model for activation of muscle thin filaments. J Mol Biol 266: 8-14. (Pubitemid 27170513)
    • (1997) Journal of Molecular Biology , vol.266 , Issue.1 , pp. 8-14
    • Vibert, P.1    Craig, R.2    Lehman, W.3
  • 38
    • 0017235497 scopus 로고
    • Movement of tropomyosin during regulation of vertebrate skeletal muscle: A simple physical model
    • Parry DAD (1976) Movement of tropomyosin during regulation of vertebrate skeletal muscle: a simple physical model. Biochem Biophys Res Commun 68:323-328.
    • (1976) Biochem Biophys Res Commun , vol.68 , pp. 323-328
    • Parry, D.A.D.1
  • 39
    • 2442419136 scopus 로고    scopus 로고
    • Ca2+induced rolling of tropomyosin in muscle thin filaments: The alpha- and beta-band hypothesis revisited
    • Holthauzen LM, Correa F, Farah CS (2004) Ca2+induced rolling of tropomyosin in muscle thin filaments: the alpha- and beta-band hypothesis revisited. J Biol Chem 279:15204-15213.
    • (2004) J Biol Chem , vol.279 , pp. 15204-15213
    • Holthauzen, L.M.1    Correa, F.2    Farah, C.S.3
  • 40
    • 0018695446 scopus 로고
    • Molecular arrangement of troponin-T in the thin filament
    • Tokyo
    • Ohtsuki I (1979) Molecular arrangement of troponin-T in the thin filament. J Biochem (Tokyo) 86:491-497.
    • (1979) J Biochem , vol.86 , pp. 491-497
    • Ohtsuki, I.1
  • 41
    • 0027535632 scopus 로고
    • Tropomodulin is associated with the free (pointed) ends of the thin filaments in rat skeletal muscle
    • Fowler VM, Sussmann MA, Miller PG, Flucher BE, Daniels MP (1993) Tropomodulin is associated with the free (pointed) ends of the thin filaments in rat skeletal muscle. J Cell Biol 120:411-420.
    • (1993) J Cell Biol , vol.120 , pp. 411-420
    • Fowler, V.M.1    Sussmann, M.A.2    Miller, P.G.3    Flucher, B.E.4    Daniels, M.P.5
  • 42
    • 0034214334 scopus 로고    scopus 로고
    • Tropomodulin-binding site mapped to residues 7-14 at the N-terminal heptad repeats of tropomyosin isoform 5
    • Vera C, Sood A, Gao KM, Yee LJ, Lin JJ, Sung LA (2000) Tropomodulin-binding site mapped to residues 7-14 at the N-terminal heptad repeats of tropomyosin isoform 5. Arch Biochem Biophys 378:16-24.
    • (2000) Arch Biochem Biophys , vol.378 , pp. 16-24
    • Vera, C.1    Sood, A.2    Gao, K.M.3    Yee, L.J.4    Lin, J.J.5    Sung, L.A.6
  • 43
    • 4243780569 scopus 로고
    • CCP4 Collaborative computational project, Number 4
    • CCP4 (1994) Collaborative computational project, Number 4. Acta Crystallogr D 760-763.
    • (1994) Acta Crystallogr D , pp. 760-763


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.