메뉴 건너뛰기




Volumn 105, Issue 20, 2008, Pages 7200-7205

Structural basis for tropomyosin overlap in thin (actin) filaments and the generation of a molecular swivel by troponin-T

Author keywords

Calcium; Cardiomyopathy; Troponin

Indexed keywords

ACTIN; CALCIUM; COILED COIL MYOSIN; TROPOMYOSIN; TROPOMYOSIN C; TROPOMYOSIN N; TROPONIN T;

EID: 44449160070     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0801950105     Document Type: Article
Times cited : (74)

References (35)
  • 1
    • 0026218642 scopus 로고
    • The molecular basis for tropomyosin isoform diversity
    • Lees-Miller JP, Helfman DM (1991) The molecular basis for tropomyosin isoform diversity. Bioessays 13:429-437.
    • (1991) Bioessays , vol.13 , pp. 429-437
    • Lees-Miller, J.P.1    Helfman, D.M.2
  • 2
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard TD, Borisy GG (2003) Cellular motility driven by assembly and disassembly of actin filaments. Cell 112:453-465.
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 3
    • 20444398071 scopus 로고    scopus 로고
    • Tropomyosin isoforms: Divining rods for actin cytoskeleton function
    • Gunning PW, Schevzov G, Kee AJ, Hardeman EC (2005) Tropomyosin isoforms: Divining rods for actin cytoskeleton function. Trends Cell Biol 15:333-341.
    • (2005) Trends Cell Biol , vol.15 , pp. 333-341
    • Gunning, P.W.1    Schevzov, G.2    Kee, A.J.3    Hardeman, E.C.4
  • 4
    • 0021914089 scopus 로고
    • Three-dimensional image analysis of the complex of thin filaments and myosin molecules from skeletal muscle. V. Assignment of actin in the actin-tropomyosin subfragment-1 complex
    • Toyoshima C, Wakabayashi T (1985) Three-dimensional image analysis of the complex of thin filaments and myosin molecules from skeletal muscle. V. Assignment of actin in the actin-tropomyosin subfragment-1 complex. J Biochem 97:245-263.
    • (1985) J Biochem , vol.97 , pp. 245-263
    • Toyoshima, C.1    Wakabayashi, T.2
  • 5
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament
    • McKillop DE, 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.E.1    Geeves, M.A.2
  • 6
    • 0035957530 scopus 로고    scopus 로고
    • 2+-induced switching of troponin and tropomyosin on actin filaments as revealed by electron cryo-microscopy
    • 2+-induced switching of troponin and tropomyosin on actin filaments as revealed by electron cryo-microscopy. J Mol Biol 308:241-261.
    • (2001) J Mol Biol , vol.308 , pp. 241-261
    • Narita, A.1    Yasunaga, T.2    Ishikawa, T.3    Mayanagi, K.4    Wakabayashi, T.5
  • 7
    • 23944457539 scopus 로고    scopus 로고
    • 2+-regulated muscle relaxation at interaction sites of troponin with actin and tropomyosin
    • 2+-regulated muscle relaxation at interaction sites of troponin with actin and tropomyosin. J Mol Biol 352:178-201.
    • (2005) J Mol Biol , vol.352 , pp. 178-201
    • Murakami, K.1
  • 8
    • 0016765447 scopus 로고
    • 14 actin binding sites on tropomyosin?
    • Stewart M, McLachlan AD (1975) 14 actin binding sites on tropomyosin? Nature 257:331-333.
    • (1975) Nature , vol.257 , pp. 331-333
    • Stewart, M.1    McLachlan, A.D.2
  • 9
    • 0000920828 scopus 로고
    • The packing of α-helices: Simple coiled-coils
    • Crick FHC (1957) The packing of α-helices: Simple coiled-coils. Acta Crystallogr 6:689-697.
    • (1957) Acta Crystallogr , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 10
    • 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
  • 11
    • 0017136639 scopus 로고
    • The 14-fold periodicity in α-tropomyosin and interaction with actin
    • McLachlan AD, Stewart M (1976) The 14-fold periodicity in α-tropomyosin and 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
  • 12
    • 0035902525 scopus 로고    scopus 로고
    • Structure of the mid-region of tropomyosin: Bending and binding sites for actin
    • Brown JH, et al (2001) Structure of the mid-region of tropomyosin: Bending and binding sites for actin. Proc Natl Acad Sci USA 98:8496-8501.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 8496-8501
    • Brown, J.H.1
  • 13
    • 0016774265 scopus 로고
    • Tropomyosin coiled-coil interactions
    • McLachlan AD, Stewart M (1975) Tropomyosin coiled-coil interactions. J Mol Biol 98:293-304.
    • (1975) J Mol Biol , vol.98 , pp. 293-304
    • McLachlan, A.D.1    Stewart, M.2
  • 14
    • 0033619726 scopus 로고    scopus 로고
    • The ends of tropomyosin are major determinants of actin affinity and myosin subfragment 1-induced binding to F-actin in the open state
    • Moraczewska J, Nicholson-Flynn K, Hitchcock-DeGregori SE (1999) The ends of tropomyosin are major determinants of actin affinity and myosin subfragment 1-induced binding to F-actin in the open state. Biochemistry 38:15885-15892.
    • (1999) Biochemistry , vol.38 , pp. 15885-15892
    • Moraczewska, J.1    Nicholson-Flynn, K.2    Hitchcock-DeGregori, S.E.3
  • 16
    • 0023091230 scopus 로고
    • Structure of co-crystals of tropomyosin and troponin
    • White SP, Cohen C, Phillips GN, Jr (1987) Structure of co-crystals of tropomyosin and troponin. Nature 325:826-828.
    • (1987) Nature , vol.325 , pp. 826-828
    • White, S.P.1    Cohen, C.2    Phillips Jr, G.N.3
  • 17
    • 0023655442 scopus 로고
    • Altered actin and troponin binding of amino-terminal variants of chicken striated muscle alpha-tropomyosin expressed in Escherichia coli
    • Hitchcock-DeGregori SE, Heald RW (1987) Altered actin and troponin binding of amino-terminal variants of chicken striated muscle alpha-tropomyosin expressed in Escherichia coli. J Biol Chem 262:9730-9735.
    • (1987) J Biol Chem , vol.262 , pp. 9730-9735
    • Hitchcock-DeGregori, S.E.1    Heald, R.W.2
  • 18
    • 0028177556 scopus 로고
    • Functional alpha-tropomyosin produced in Escherichia coli. A dipeptide extension can substitute the amino-terminal acetyl group
    • Monteiro PB, Lataro RC, Ferro JA, Reinach FC (1994) Functional alpha-tropomyosin produced in Escherichia coli. A dipeptide extension can substitute the amino-terminal acetyl group. J Biol Chem 269:10461-10466.
    • (1994) J Biol Chem , vol.269 , pp. 10461-10466
    • Monteiro, P.B.1    Lataro, R.C.2    Ferro, J.A.3    Reinach, F.C.4
  • 19
    • 0037188485 scopus 로고    scopus 로고
    • The crystal structure of the C-terminal fragment of striated-muscle alpha-tropomyosin reveals a key troponin T recognition site
    • Li Y, et al. (2002) The crystal structure of the C-terminal fragment of striated-muscle alpha-tropomyosin reveals a key troponin T recognition site. Proc Natl Acad Sci USA 99:7378-7383.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 7378-7383
    • Li, Y.1
  • 20
    • 0037414799 scopus 로고    scopus 로고
    • Folding and function of the troponin tail domain. Effects of cardiomyopathic troponin T mutations
    • Hinkle A, Tobacman LS (2003) Folding and function of the troponin tail domain. Effects of cardiomyopathic troponin T mutations. J Biol Chem 278:506-513.
    • (2003) J Biol Chem , vol.278 , pp. 506-513
    • Hinkle, A.1    Tobacman, L.S.2
  • 22
    • 0019424237 scopus 로고
    • Fragments of rabbit striated muscle alphatropomyosin. I. Preparation and characterization
    • Pato MD, Mak AS, Smillie LB (1981) Fragments of rabbit striated muscle alphatropomyosin. I. Preparation and characterization. J Biol Chem 256:593-601.
    • (1981) J Biol Chem , vol.256 , pp. 593-601
    • Pato, M.D.1    Mak, A.S.2    Smillie, L.B.3
  • 23
    • 0030067632 scopus 로고    scopus 로고
    • Mapping the functional domains within the carboxyl terminus of alpha-tropomyosin encoded by the alternatively spliced ninth exon
    • Hammell RL, Hitchcock-DeGregori SE (1996) Mapping the functional domains within the carboxyl terminus of alpha-tropomyosin encoded by the alternatively spliced ninth exon. J Biol Chem 271:4236-4242.
    • (1996) J Biol Chem , vol.271 , pp. 4236-4242
    • Hammell, R.L.1    Hitchcock-DeGregori, S.E.2
  • 24
    • 33750306274 scopus 로고    scopus 로고
    • Solution NMR structure of the junction between tropomyosin molecules: Implications for actin binding and regulation
    • Greenfield NJ, et al. (2006) Solution NMR structure of the junction between tropomyosin molecules: Implications for actin binding and regulation. J Mol Biol 364:80-96.
    • (2006) J Mol Biol , vol.364 , pp. 80-96
    • Greenfield, N.J.1
  • 26
    • 0033985268 scopus 로고    scopus 로고
    • Crystal structure of tropomyosin at 7 Angstroms resolution
    • Whitby FG, Phillips GN, Jr (2000) Crystal structure of tropomyosin at 7 Angstroms resolution. Proteins 38:49-59.
    • (2000) Proteins , vol.38 , pp. 49-59
    • Whitby, F.G.1    Phillips Jr, G.N.2
  • 27
    • 0030048070 scopus 로고    scopus 로고
    • Protein-protein interactions in the rigor actomyosin complex
    • Milligan RA (1996) Protein-protein interactions in the rigor actomyosin complex. Proc Natl Acad Sci USA 93:21-26.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 21-26
    • Milligan, R.A.1
  • 28
    • 0037119477 scopus 로고    scopus 로고
    • A modulatory role for the troponin T tail domain in thin filament regulation
    • Maytum R, Geeves MA, Lehrer SS (2002) A modulatory role for the troponin T tail domain in thin filament regulation. J Biol Chem 277:29774-29780.
    • (2002) J Biol Chem , vol.277 , pp. 29774-29780
    • Maytum, R.1    Geeves, M.A.2    Lehrer, S.S.3
  • 29
    • 30044447175 scopus 로고    scopus 로고
    • Structure of the mid-region of tropomyosin: Bending and binding sites for actin
    • Brown JH, et al. (2005) Structure of the mid-region of tropomyosin: Bending and binding sites for actin. Proc Natl Acad Sci USA 102:18878-18883.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 18878-18883
    • Brown, J.H.1
  • 30
    • 33747123989 scopus 로고    scopus 로고
    • 2+-dependent regulation of striated muscle thin filaments
    • 2+-dependent regulation of striated muscle thin filaments. Biochemistry 45:9550-9558.
    • (2006) Biochemistry , vol.45 , pp. 9550-9558
    • Sakuma, A.1
  • 32
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and for locating errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M (1991) Improved methods for building protein models in electron density maps and for locating errors in these models. Acta Crystallogr A 47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 33
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger AT, et al. (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr D 54:905-921.
    • (1998) Acta Crystallogr D , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 34
    • 0028103275 scopus 로고    scopus 로고
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D 50:760-763.
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D 50:760-763.
  • 35
    • 0036445512 scopus 로고    scopus 로고
    • Analysis of α-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation
    • Strelkov SV, Burkhard P (2002) Analysis of α-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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.