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Volumn 98, Issue 4, 1999, Pages 537-546

Structure of the α-actinin rod: Molecular basis for cross-linking of actin filaments

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA ACTININ;

EID: 0033588277     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81981-9     Document Type: Article
Times cited : (221)

References (61)
  • 1
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton G.J. (1993). ALSCRIPT: a tool to format multiple sequence alignments. Prot. Eng. 6, 37-40.
    • (1993) Prot. Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 2
    • 0031281898 scopus 로고    scopus 로고
    • Zyxin: Zinc fingers at sites of cell adhesion
    • Beckerle, M.C. (1997). Zyxin: zinc fingers at sites of cell adhesion. Bioessays 19, 949-957.
    • (1997) Bioessays , vol.19 , pp. 949-957
    • Beckerle, M.C.1
  • 3
    • 0026786782 scopus 로고
    • Cloning and characterization of two human skeletal muscle α-actinin genes located on chromosomes 1 and 11
    • Beggs, A.H., Byers, T.J., Knoll, J.H., Boyce, P.M., Bruns, G.A., and Kunkel, L.M. (1992). Cloning and characterization of two human skeletal muscle α-actinin genes located on chromosomes 1 and 11. J. Biol. Chem. 267, 9281-9288.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9281-9288
    • Beggs, A.H.1    Byers, T.J.2    Knoll, J.H.3    Boyce, P.M.4    Bruns, G.A.5    Kunkel, L.M.6
  • 8
    • 0026672861 scopus 로고
    • Association of intercellular adhesion molecule-1 (ICAM-1) with actincontaining cytoskeleton and α-actinin
    • Carpen, O., Pallai, P., Staunton, D.E., and Springer, T.A. (1992). Association of intercellular adhesion molecule-1 (ICAM-1) with actincontaining cytoskeleton and α-actinin. J. Cell Biol. 118,1223-1234.
    • (1992) J. Cell Biol. , vol.118 , pp. 1223-1234
    • Carpen, O.1    Pallai, P.2    Staunton, D.E.3    Springer, T.A.4
  • 9
    • 0033081137 scopus 로고    scopus 로고
    • How many water molecules can be detected by protein crystallography?
    • Carugo, O., and Bordo, D. (1999). How many water molecules can be detected by protein crystallography?. Acta Crystallogr. D 55, 479-483.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 479-483
    • Carugo, O.1    Bordo, D.2
  • 10
    • 0028785252 scopus 로고
    • Does Vav bind to F-actin through a CH domain?
    • Castresana, J., and Saraste, M. (1995). Does Vav bind to F-actin through a CH domain? FEBS Lett. 374, 149-151.
    • (1995) FEBS Lett. , vol.374 , pp. 149-151
    • Castresana, J.1    Saraste, M.2
  • 11
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (Collaborative Computing Project No. 4). (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 12
  • 13
    • 0024299114 scopus 로고
    • Actinins and the DM D protein contain spectrin-like repeats
    • Davison, M.D., and Critchley, D.R. (1988). α-Actinins and the DM D protein contain spectrin-like repeats. Cell 52, 159-160.
    • (1988) Cell , vol.52 , pp. 159-160
    • Davison, M.D.1    Critchley, D.R.2
  • 14
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de la Fortelle, E., and Bricogne, G. (1997). Maximum-likelihood heavy atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 15
    • 0028971161 scopus 로고
    • Structural superposition of proteins with unknown alignment and detection of topological similarity using a sixdimensional search algorithm
    • Diederichs, K. (1995). Structural superposition of proteins with unknown alignment and detection of topological similarity using a sixdimensional search algorithm. Proteins 23, 187-195.
    • (1995) Proteins , vol.23 , pp. 187-195
    • Diederichs, K.1
  • 17
    • 0030750630 scopus 로고    scopus 로고
    • Further analysis of the role of spectrin repeat motifs in α-actinin dimer formation
    • Flood, G., Rowe, A.J., Critchley, D.R., and Gratzer, W.B. (1997). Further analysis of the role of spectrin repeat motifs in α-actinin dimer formation. Eur. Biophys. J. 25, 431-435.
    • (1997) Eur. Biophys. J. , vol.25 , pp. 431-435
    • Flood, G.1    Rowe, A.J.2    Critchley, D.R.3    Gratzer, W.B.4
  • 18
    • 0030818593 scopus 로고    scopus 로고
    • PHASES-95: A program package for the processing and analysis of diffraction data from macromolecules
    • C.W. Carter and R.M. Sweet, eds. (Orlando, FL: Academic Press)
    • Furey, W.B., and Swaminathan, S. (1997). PHASES-95: a program package for the processing and analysis of diffraction data from macromolecules. In Methods in Enzymology, Vol. 277, C.W. Carter and R.M. Sweet, eds. (Orlando, FL: Academic Press), pp. 590-620.
    • (1997) Methods in Enzymology , vol.277 , pp. 590-620
    • Furey, W.B.1    Swaminathan, S.2
  • 21
    • 0033588274 scopus 로고    scopus 로고
    • Structures of two repeats of spectrin suggest models for flexibility
    • Grum, V.L., Li, D., MacDonald, R.I., and Mondragën, A. (1999). Structures of two repeats of spectrin suggest models for flexibility. Cell 98, this issue, 523-535.
    • (1999) Cell , vol.98 , pp. 523-535
    • Grum, V.L.1    Li, D.2    MacDonald, R.I.3    Mondragën, A.4
  • 22
    • 0029908326 scopus 로고    scopus 로고
    • Binding of the cytoplasmic domain of intercellular adhesion molecule-2 (1CAM-2) to α-actinin
    • Heiska, l., Kantor, C., Parr, T., Critchley, D.R., Vilja, P., Gahmberg, C.G., and Carpen, O. (1996). Binding of the cytoplasmic domain of intercellular adhesion molecule-2 (1CAM-2) to α-actinin. J. Biol. Chem. 277, 26214-26219.
    • (1996) J. Biol. Chem. , vol.277 , pp. 26214-26219
    • Heiska, L.1    Kantor, C.2    Parr, T.3    Critchley, D.R.4    Vilja, P.5    Gahmberg, C.G.6    Carpen, O.7
  • 23
    • 0026605537 scopus 로고
    • CLUSTAL V: Improved software for multiple sequence alignment
    • Higgins, D.G., Bleasby, A.J., and Fuchs, R. (1992). CLUSTAL V: improved software for multiple sequence alignment. Comput. Appl. Biosci. 8, 189-191.
    • (1992) Comput. Appl. Biosci. , vol.8 , pp. 189-191
    • Higgins, D.G.1    Bleasby, A.J.2    Fuchs, R.3
  • 24
    • 0022534722 scopus 로고
    • Interaction of plasma membrane fibronectin receptor with talin-a transmembrane linkage
    • Horwitz, A., Duggan, K., Buck, C., Beckerle, M.C., and Burridge, K. (1986). Interaction of plasma membrane fibronectin receptor with talin-a transmembrane linkage. Nature 320, 531-533.
    • (1986) Nature , vol.320 , pp. 531-533
    • Horwitz, A.1    Duggan, K.2    Buck, C.3    Beckerle, M.C.4    Burridge, K.5
  • 25
    • 0024278676 scopus 로고
    • Substructure and higher structure of chicken smooth muscle α-actinin molecule
    • Imamura, M., Endo, T., Kuroda, M., Tanaka,T., and Masaki, T. (1988). Substructure and higher structure of chicken smooth muscle α-actinin molecule. J. Biol. Chem. 263, 7800-7805.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7800-7805
    • Imamura, M.1    Endo, T.2    Kuroda, M.3    Tanaka, T.4    Masaki, T.5
  • 26
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones, S., and Thornton, ü.M. (1996). Principles of protein-protein interactions. Proc. Natl. Acad. Sci. USA 93, 13-20.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, M.2
  • 27
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowen, S.W., and Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of 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    Cowen, S.W.3    Kjeldgaard, M.4
  • 28
    • 0025750757 scopus 로고
    • Properties of the spectrin-like structural element of smooth-muscle α-actinin
    • Kahana, E., and Gratzer, W.B. (1991). Properties of the spectrin-like structural element of smooth-muscle α-actinin. Cell Motil. Cytoskeleton 20, 242-248.
    • (1991) Cell Motil. Cytoskeleton , vol.20 , pp. 242-248
    • Kahana, E.1    Gratzer, W.B.2
  • 29
    • 0032514952 scopus 로고    scopus 로고
    • Orientation, positional, additivity, and oligomerization-state effects of interhelical ion pairs in .α-helical coiled-coils
    • Kohn, W.D., Kay, C.M., and Hodges, R.S. (1998). Orientation, positional, additivity, and oligomerization-state effects of interhelical ion pairs in .α-helical coiled-coils. J. Mol. Biol. 283, 993-1012.
    • (1998) J. Mol. Biol. , vol.283 , pp. 993-1012
    • Kohn, W.D.1    Kay, C.M.2    Hodges, R.S.3
  • 30
    • 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
  • 31
    • 0028208411 scopus 로고
    • Conformational change of skeletal muscle α-actinin induced by salt
    • Kuroda, M., Kohira, Y., and Sasaki, M. (1994). Conformational change of skeletal muscle α-actinin induced by salt. Biochim. Biophys. Acta. 7205, 97-104.
    • (1994) Biochim. Biophys. Acta. , vol.7205 , pp. 97-104
    • Kuroda, M.1    Kohira, Y.2    Sasaki, M.3
  • 32
    • 0022398533 scopus 로고
    • Properties of two isoforms of human blood platelet α-actinin
    • Landon, F., Gache, Y., Touitou, H., and Olomucki, A. (1985). Properties of two isoforms of human blood platelet α-actinin. Eur. J. Biochem. 153, 231-237.
    • (1985) Eur. J. Biochem. , vol.153 , pp. 231-237
    • Landon, F.1    Gache, Y.2    Touitou, H.3    Olomucki, A.4
  • 33
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., Mac Arthur, M.W., Moss, D.S., and Thornton, ü.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Mac Arthur, M.W.2    Moss, D.S.3    Thornton, M.4
  • 34
    • 0026565486 scopus 로고
    • Energetic contribution of solvent-exposed ion pairs to α-helix structure
    • Lyu, P.C., Gans, P.J., and Kallenbach, N.R. (1992). Energetic contribution of solvent-exposed ion pairs to α-helix structure. J. Mol. Biol. 223, 343-350.
    • (1992) J. Mol. Biol. , vol.223 , pp. 343-350
    • Lyu, P.C.1    Gans, P.J.2    Kallenbach, N.R.3
  • 35
    • 0016774265 scopus 로고
    • Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure
    • McLachlan, A.D., and 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
  • 36
    • 0028057108 scopus 로고
    • Raster3D Version 2.0: A program for photorealistic molecular graphics
    • Merritt, E.A., and Murphy, M.E.P. (1994). Raster3D Version 2.0: a program for photorealistic molecular graphics. Acta Crystallogr. D 50, 869-873.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 38
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A., and Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 39
    • 0031560933 scopus 로고    scopus 로고
    • The N-terminal Z repeat 5 of connectin/titin binds to the C-terminal region of α-actinin
    • Ohtsuka, H., Yajami, H., Maruyama, K., and Kimura, S. (1997). The N-terminal Z repeat 5 of connectin/titin binds to the C-terminal region of α-actinin. Biochem. Biophys. Res. Commun. 235, 1-3.
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 1-3
    • Ohtsuka, H.1    Yajami, H.2    Maruyama, K.3    Kimura, S.4
  • 40
    • 0025291522 scopus 로고
    • An interaction between α-actinin and the β1 integrin subunit in vitro
    • Otey, C.A., Pavalko, F.M., and Burridge, K. (1990). An interaction between α-actinin and the β1 integrin subunit in vitro. J. Cell Biol. 111, 721-729.
    • (1990) J. Cell Biol. , vol.111 , pp. 721-729
    • Otey, C.A.1    Pavalko, F.M.2    Burridge, K.3
  • 41
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 42
    • 0000649842 scopus 로고    scopus 로고
    • Improved structure refinement through maximum likelihood
    • Pannu, N.S., and Read, R.J. (1996). Improved structure refinement through maximum likelihood. Acta Crystallogr. A 52, 659-668.
    • (1996) Acta Crystallogr. A , vol.52 , pp. 659-668
    • Pannu, N.S.1    Read, R.J.2
  • 43
    • 0028329918 scopus 로고
    • Release of proteins and peptides from fusion proteins using a recombinant plant virus proteinase
    • Parks, T.D., Leuther, K.K., Howard, E.D., Johnston, S.A., and Dougherty, W.G. (1994). Release of proteins and peptides from fusion proteins using a recombinant plant virus proteinase. Anal. Biochem. 276, 413-417.
    • (1994) Anal. Biochem. , vol.276 , pp. 413-417
    • Parks, T.D.1    Leuther, K.K.2    Howard, E.D.3    Johnston, S.A.4    Dougherty, W.G.5
  • 44
    • 0031239149 scopus 로고    scopus 로고
    • Evolution of the spectrin repeat
    • Pascual, J., Castresana, J., and Saraste, M. (1997a). Evolution of the spectrin repeat. Bioessays 19, 811-817.
    • (1997) Bioessays , vol.19 , pp. 811-817
    • Pascual, J.1    Castresana, J.2    Saraste, M.3
  • 45
    • 0031592935 scopus 로고    scopus 로고
    • Solution structure of the spectrin repeat: A left-handed antiparallel triple-helical coiled-coil
    • Pascual, J., Pfuhl, M., Walther, D., Saraste, M., and Nilges, M. (1997b). Solution structure of the spectrin repeat: a left-handed antiparallel triple-helical coiled-coil. J. Mol. Biol. 273, 740-751.
    • (1997) J. Mol. Biol. , vol.273 , pp. 740-751
    • Pascual, J.1    Pfuhl, M.2    Walther, D.3    Saraste, M.4    Nilges, M.5
  • 46
    • 0029074732 scopus 로고
    • The cytoplasmic domain of L-selectin interacts with cytoskeletal proteins via α-actinin: Receptor positioning in microvilli does not require interaction with α-actinin
    • Pavalko, P.M., Walker, D.M., Graham, l., Goheen, M., Doerschuk, C.M., and Kansas, G.S. (1995). The cytoplasmic domain of L-selectin interacts with cytoskeletal proteins via α-actinin: receptor positioning in microvilli does not require interaction with α-actinin. J. Cell Biol. 729, 1155-1164.
    • (1995) J. Cell Biol. , vol.729 , pp. 1155-1164
    • Pavalko, P.M.1    Walker, D.M.2    Graham, L.3    Goheen, M.4    Doerschuk, C.M.5    Kansas, G.S.6
  • 47
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read, R.J. (1986). Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A 42, 140-149.
    • (1986) Acta Crystallogr. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 48
    • 0033582763 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of spectrin repeats: Low unfolding forces in helix bundles
    • Rief, M., Pascual, J., Saraste, M., and Gaub, H.E. (1999). Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles. J. Mol. Biol. 286, 553-561.
    • (1999) J. Mol. Biol. , vol.286 , pp. 553-561
    • Rief, M.1    Pascual, J.2    Saraste, M.3    Gaub, H.E.4
  • 49
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A., and Blundell, T.L. (1993). Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 50
    • 0021272595 scopus 로고
    • Erythrocyte spectrin is comprised of many homologous triple helical segments
    • Speicher, D.W., and Marches!, V.T. (1984). Erythrocyte spectrin is comprised of many homologous triple helical segments. Nature 37 7, 177-180.
    • (1984) Nature , vol.311 , pp. 177-180
    • Speicher, D.W.1    Marches, V.T.2
  • 51
    • 0026653822 scopus 로고
    • Properties of human red cell spectrin heterodimer (side-to-side) assembly and identification of an essential nucleation site
    • Speicher, D.W., Weglarz, l., and DeSilva, T.M. (1992). Properties of human red cell spectrin heterodimer (side-to-side) assembly and identification of an essential nucleation site. J. Biol. Chem. 267, 14775-14782.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14775-14782
    • Speicher, D.W.1    Weglarz, L.2    Desilva, T.M.3
  • 52
    • 0027474019 scopus 로고
    • Projection image of smooth muscle α-actinin from two-dimensional crystals formed on positively charged lipid layers
    • Taylor, K.A., and Taylor, D.W. (1993). Projection image of smooth muscle α-actinin from two-dimensional crystals formed on positively charged lipid layers. J. Mol. Biol. 230, 196-205.
    • (1993) J. Mol. Biol. , vol.230 , pp. 196-205
    • Taylor, K.A.1    Taylor, D.W.2
  • 53
    • 0028985239 scopus 로고
    • The C-terminal domain of α-spectrin is structurally related to calmodulin
    • Trave, G., Pastore, A., Hyvonen, M., and Saraste, M. (1995). The C-terminal domain of α-spectrin is structurally related to calmodulin. Eur. J. Biochem. 227, 35-42.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 35-42
    • Trave, G.1    Pastore, A.2    Hyvonen, M.3    Saraste, M.4
  • 54
    • 0028000263 scopus 로고
    • Interchain binding at the tail end of the Drosophila spectrin molecule
    • Viel, A., and Branton, D. (1994). Interchain binding at the tail end of the Drosophila spectrin molecule. Proc. Natl. Acad. Sci. USA 91, 10839-10843.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10839-10843
    • Viel, A.1    Branton, D.2
  • 56
  • 57
    • 0030740644 scopus 로고    scopus 로고
    • Flexibility and fine structure of smooth-muscle α-actinin
    • Winkler, J., Lunsdorf, H., and Jockusch, B.M. (1997). Flexibility and fine structure of smooth-muscle α-actinin. Eur. J. Biochem. 248, 193-199.
    • (1997) Eur. J. Biochem. , vol.248 , pp. 193-199
    • Winkler, J.1    Lunsdorf, H.2    Jockusch, B.M.3
  • 58
    • 0031013896 scopus 로고    scopus 로고
    • Competitive binding of α-actinin and calmodulin to the NMDA receptor
    • Wyszynski, M., Lin, J., Rao, A., Nigh, E., Beggs, A.H., Craig, A.M., and Sheng, M. (1997). Competitive binding of α-actinin and calmodulin to the NMDA receptor. Nature 385, 439-442.
    • (1997) Nature , vol.385 , pp. 439-442
    • Wyszynski, M.1    Lin, J.2    Rao, A.3    Nigh, E.4    Beggs, A.H.5    Craig, A.M.6    Sheng, M.7
  • 59
    • 0030827949 scopus 로고    scopus 로고
    • Actinin-associated LIM protein: Identification of a domain interaction between PDZ and spectrin-like repeat motifs
    • Xia, H., Winokur, S.T., Kuo, W.L., Altherr, M.R., and Bredt, D.S. (1997). Actinin-associated LIM protein: identification of a domain interaction between PDZ and spectrin-like repeat motifs. J. Cell Biol. 739, 507-515.
    • (1997) J. Cell Biol. , vol.739 , pp. 507-515
    • Xia, H.1    Winokur, S.T.2    Kuo, W.L.3    Altherr, M.R.4    Bredt, D.S.5
  • 61
    • 0032536770 scopus 로고    scopus 로고
    • Molecular structure of the sarcomeric Z-disk: Two types of titin interactions lead to an asymmetrical sorting of α-actinin
    • Young, P., Ferguson, C., Banuelos, S., and Gautel, M. (1998). Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of α-actinin. EM BO J. 77,1614-1624.
    • (1998) EMBO J. , vol.77 , pp. 1614-1624
    • Young, P.1    Ferguson, C.2    Banuelos, S.3    Gautel, M.4


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