메뉴 건너뛰기




Volumn 353, Issue 3, 2005, Pages 613-628

Skip residues and charge interactions in myosin II coiled-coils: Implications for molecular packing

Author keywords

Bipolar myosin filaments; Coiled coil skip residues; Myosin filament structure; Myosin II rod sequences; Side polar myosin filaments

Indexed keywords

MYOSIN; MYOSIN 2; UNCLASSIFIED DRUG;

EID: 26244466046     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.08.010     Document Type: Article
Times cited : (41)

References (37)
  • 1
    • 0019873637 scopus 로고
    • Three-dimensional structure of the vertebrate muscle A-band. III. M-region structure and myosin filament symmetry
    • P.K. Luther, P.M. Munro, and J.M. Squire Three-dimensional structure of the vertebrate muscle A-band. III. M-region structure and myosin filament symmetry J. Mol. Biol. 151 1981 703 730
    • (1981) J. Mol. Biol. , vol.151 , pp. 703-730
    • Luther, P.K.1    Munro, P.M.2    Squire, J.M.3
  • 2
    • 0030967587 scopus 로고    scopus 로고
    • Architecture and function in the muscle sarcomere
    • J.M. Squire Architecture and function in the muscle sarcomere Curr. Opin. Struct. Biol. 7 1997 247 257
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 247-257
    • Squire, J.M.1
  • 3
    • 0031079847 scopus 로고    scopus 로고
    • The swinging lever-arm hypothesis of muscle contraction
    • K.C. Holmes The swinging lever-arm hypothesis of muscle contraction Curr. Biol. 7 1997 R112 R118
    • (1997) Curr. Biol. , vol.7
    • Holmes, K.C.1
  • 4
    • 85012414651 scopus 로고
    • Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscle
    • H.E. Huxley Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscle J. Mol. Biol. 77 1963 281 308
    • (1963) J. Mol. Biol. , vol.77 , pp. 281-308
    • Huxley, H.E.1
  • 5
    • 0015505937 scopus 로고
    • Structural basis of contraction in vertebrate smooth muscle
    • J.V. Small, and J.M. Squire Structural basis of contraction in vertebrate smooth muscle J. Mol. Biol. 67 1972 117 149
    • (1972) J. Mol. Biol. , vol.67 , pp. 117-149
    • Small, J.V.1    Squire, J.M.2
  • 6
    • 0017672926 scopus 로고
    • Assembly of smooth muscle myosin into side-polar filaments
    • R. Craig, and J. Megerman Assembly of smooth muscle myosin into side-polar filaments J. Cell. Biol. 75 1977 990 996
    • (1977) J. Cell. Biol. , vol.75 , pp. 990-996
    • Craig, R.1    Megerman, J.2
  • 7
    • 0019975166 scopus 로고
    • Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle
    • A.D. McLachlan, and J. Karn Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle Nature 299 1982 226 231
    • (1982) Nature , vol.299 , pp. 226-231
    • McLachlan, A.D.1    Karn, J.2
  • 8
    • 0026700379 scopus 로고
    • Role of the COOH-terminal nonhelical tailpiece in the assembly of a vertebrate nonmuscle myosin rod
    • T.P. Hodge, R. Cross, and J. Kendrick-Jones Role of the COOH-terminal nonhelical tailpiece in the assembly of a vertebrate nonmuscle myosin rod J. Cell. Biol. 118 1992 1085 1095
    • (1992) J. Cell. Biol. , vol.118 , pp. 1085-1095
    • Hodge, T.P.1    Cross, R.2    Kendrick-Jones, J.3
  • 9
    • 0000920828 scopus 로고
    • The packing of alpha-helices: Simple coiled-coils
    • F.H.C. Crick The packing of alpha-helices: simple coiled-coils Acta Crystallog. 6 1953 689 697
    • (1953) Acta Crystallog. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 10
    • 0025601653 scopus 로고
    • Skip residues correlate with bends in the myosin tail
    • G. Offer Skip residues correlate with bends in the myosin tail J. Mol. Biol. 216 1990 213 218
    • (1990) J. Mol. Biol. , vol.216 , pp. 213-218
    • Offer, G.1
  • 11
    • 85010249552 scopus 로고
    • The low-angle x-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor
    • H.E. Huxley, and W. Brown The low-angle x-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor J. Mol. Biol. 30 1967 383 434
    • (1967) J. Mol. Biol. , vol.30 , pp. 383-434
    • Huxley, H.E.1    Brown, W.2
  • 12
    • 0016610095 scopus 로고
    • X-ray evidence for conformational changes in the myosin filaments of vertebrate striated muscle
    • J.C. Haselgrove X-ray evidence for conformational changes in the myosin filaments of vertebrate striated muscle J. Mol. Biol. 92 1975 113 143
    • (1975) J. Mol. Biol. , vol.92 , pp. 113-143
    • Haselgrove, J.C.1
  • 13
    • 0015227575 scopus 로고
    • General model for the structure of all myosin-containing filaments
    • J.M. Squire General model for the structure of all myosin-containing filaments Nature 233 1971 457 462
    • (1971) Nature , vol.233 , pp. 457-462
    • Squire, J.M.1
  • 16
    • 0017074536 scopus 로고
    • Structure of the cross-striated adductor muscle of the scallop
    • B.M. Millman, and P.M. Bennett Structure of the cross-striated adductor muscle of the scallop J. Mol. Biol. 103 1976 439 467
    • (1976) J. Mol. Biol. , vol.103 , pp. 439-467
    • Millman, B.M.1    Bennett, P.M.2
  • 17
    • 0017756673 scopus 로고
    • Light meromyosin paracrystal formation
    • P.K. Chowrashi, and F.A. Pepe Light meromyosin paracrystal formation J. Cell. Biol. 74 1977 136 152
    • (1977) J. Cell. Biol. , vol.74 , pp. 136-152
    • Chowrashi, P.K.1    Pepe, F.A.2
  • 19
    • 0033118853 scopus 로고    scopus 로고
    • Assembly of thick filaments and myofibrils occurs in the absence of the myosin head
    • R.M. Cripps, J.A. Suggs, and S.I. Bernstein Assembly of thick filaments and myofibrils occurs in the absence of the myosin head EMBO J. 18 1999 1793 1804
    • (1999) EMBO J. , vol.18 , pp. 1793-1804
    • Cripps, R.M.1    Suggs, J.A.2    Bernstein, S.I.3
  • 20
    • 0023369713 scopus 로고
    • Crystalline tubes of myosin subfragment-2 showing the coiled-coil and molecular interaction geometry
    • R.A. Quinlan, and M. Stewart Crystalline tubes of myosin subfragment-2 showing the coiled-coil and molecular interaction geometry J. Cell. Biol. 105 1987 403 415
    • (1987) J. Cell. Biol. , vol.105 , pp. 403-415
    • Quinlan, R.A.1    Stewart, M.2
  • 21
    • 0021152449 scopus 로고
    • Structural implications of the myosin amino acid sequence
    • A.D. McLachlan Structural implications of the myosin amino acid sequence Annu. Rev. Biophys. Bioeng. 13 1984 167 189
    • (1984) Annu. Rev. Biophys. Bioeng. , vol.13 , pp. 167-189
    • McLachlan, A.D.1
  • 23
    • 0015833973 scopus 로고
    • General model of myosin filament structure. 3. Molecular packing arrangements in myosin filaments
    • J.M. Squire General model of myosin filament structure. 3. Molecular packing arrangements in myosin filaments J. Mol. Biol. 77 1973 291 323
    • (1973) J. Mol. Biol. , vol.77 , pp. 291-323
    • Squire, J.M.1
  • 24
    • 0029586906 scopus 로고
    • Packing of alpha-helical coiled-coil myosin rods in vertebrate muscle thick filaments
    • M.W. Chew, and J.M. Squire Packing of alpha-helical coiled-coil myosin rods in vertebrate muscle thick filaments J. Struct. Biol. 115 1995 233 249
    • (1995) J. Struct. Biol. , vol.115 , pp. 233-249
    • Chew, M.W.1    Squire, J.M.2
  • 25
    • 0018328198 scopus 로고
    • Structure of the backbone in myosin filaments of muscle
    • J.S. Wray Structure of the backbone in myosin filaments of muscle Nature 277 1979 37 40
    • (1979) Nature , vol.277 , pp. 37-40
    • Wray, J.S.1
  • 26
    • 0018804583 scopus 로고
    • Distribution of light chains in fast skeletal myosin
    • S. Lowey, P.A. Benefield, L. Silberstein, and L.M. Lang Distribution of light chains in fast skeletal myosin Nature 282 1979 522 524
    • (1979) Nature , vol.282 , pp. 522-524
    • Lowey, S.1    Benefield, P.A.2    Silberstein, L.3    Lang, L.M.4
  • 27
    • 0017336444 scopus 로고
    • Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility
    • A.G. Weeds, and B. Pope Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility J. Mol. Biol. 111 1977 129 157
    • (1977) J. Mol. Biol. , vol.111 , pp. 129-157
    • Weeds, A.G.1    Pope, B.2
  • 28
    • 0017325762 scopus 로고
    • Fine structure of the A-band in cryo-sections. the structure of the A-band of human skeletal muscle fibres from ultra-thin cryo-sections negatively stained
    • M. Sjostrom, and J.M. Squire Fine structure of the A-band in cryo-sections. The structure of the A-band of human skeletal muscle fibres from ultra-thin cryo-sections negatively stained J. Mol. Biol. 109 1977 49 68
    • (1977) J. Mol. Biol. , vol.109 , pp. 49-68
    • Sjostrom, M.1    Squire, J.M.2
  • 29
    • 0021103673 scopus 로고
    • Periodic features in the amino acid sequence of nematode myosin rod
    • A.D. McLachlan, and J. Karn Periodic features in the amino acid sequence of nematode myosin rod J. Mol. Biol. 164 1983 605 626
    • (1983) J. Mol. Biol. , vol.164 , pp. 605-626
    • McLachlan, A.D.1    Karn, J.2
  • 30
    • 0015218661 scopus 로고
    • Geometry of the myosin dimer
    • M. Burke, and W.F. Harrington Geometry of the myosin dimer Nature 233 1971 140 142
    • (1971) Nature , vol.233 , pp. 140-142
    • Burke, M.1    Harrington, W.F.2
  • 31
    • 0026772937 scopus 로고
    • Molecular interactions in myosin assembly. Role of the 28-residue charge repeat in the rod
    • S.J. Atkinson, and M. Stewart Molecular interactions in myosin assembly. Role of the 28-residue charge repeat in the rod J. Mol. Biol. 226 1992 7 13
    • (1992) J. Mol. Biol. , vol.226 , pp. 7-13
    • Atkinson, S.J.1    Stewart, M.2
  • 32
    • 0022544420 scopus 로고
    • Solubility-determining domain of smooth muscle myosin rod
    • R.A. Cross, and J. Vandekerckhove Solubility-determining domain of smooth muscle myosin rod FEBS Letters 200 1986 355 360
    • (1986) FEBS Letters , vol.200 , pp. 355-360
    • Cross, R.A.1    Vandekerckhove, J.2
  • 33
    • 0036446688 scopus 로고    scopus 로고
    • Structure and nucleotide-dependent changes of thick filaments in relaxed and rigor plaice fin muscle
    • M.E. Cantino, M.W. Chew, P.K. Luther, E. Morris, and J.M. Squire Structure and nucleotide-dependent changes of thick filaments in relaxed and rigor plaice fin muscle J. Struct. Biol. 137 2002 164 175
    • (2002) J. Struct. Biol. , vol.137 , pp. 164-175
    • Cantino, M.E.1    Chew, M.W.2    Luther, P.K.3    Morris, E.4    Squire, J.M.5
  • 34
    • 0017234893 scopus 로고
    • The location of C-protein in rabbit skeletal muscle
    • R. Craig, and G. Offer The location of C-protein in rabbit skeletal muscle Proc. Roy. Soc. ser. B 192 1976 451 461
    • (1976) Proc. Roy. Soc. Ser. B , vol.192 , pp. 451-461
    • Craig, R.1    Offer, G.2
  • 35
    • 0015506342 scopus 로고
    • Cross-bridges on self-assembled smooth muscle myosin filaments
    • A. Sobieszek Cross-bridges on self-assembled smooth muscle myosin filaments J. Mol. Biol. 70 1972 741 744
    • (1972) J. Mol. Biol. , vol.70 , pp. 741-744
    • Sobieszek, A.1
  • 36
    • 0029987687 scopus 로고    scopus 로고
    • Myosin filament structure in vertebrate smooth muscle
    • J.Q. Xu, B.A. Harder, P. Uman, and R. Craig Myosin filament structure in vertebrate smooth muscle J. Cell. Biol. 134 1996 53 66
    • (1996) J. Cell. Biol. , vol.134 , pp. 53-66
    • Xu, J.Q.1    Harder, B.A.2    Uman, P.3    Craig, R.4
  • 37
    • 0026011489 scopus 로고
    • A nucleation-elongation mechanism for the self-assembly of side polar sheets of smooth muscle myosin
    • R.A. Cross, M.A. Geeves, and J. Kendrick-Jones A nucleation-elongation mechanism for the self-assembly of side polar sheets of smooth muscle myosin EMBO J. 10 1991 747 756
    • (1991) EMBO J. , vol.10 , pp. 747-756
    • Cross, R.A.1    Geeves, M.A.2    Kendrick-Jones, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.