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Volumn 342, Issue 5, 2004, Pages 1637-1646

Molecular structure of the rod domain of Dictyostelium filamin

Author keywords

ABP120; actin; ddFLN; filamin; structure

Indexed keywords

DIMER; F ACTIN; FILAMIN; IMMUNOGLOBULIN; PROTEIN;

EID: 4444309520     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.08.017     Document Type: Article
Times cited : (37)

References (34)
  • 2
    • 0029859177 scopus 로고    scopus 로고
    • The role of the cortical cytoskeleton: F-actin crosslinking proteins protect against osmotic stress, ensure cell size, cell shape and motility, and contribute to phagocytosis and development
    • F. Rivero, B. Köppel, B. Peracino, S. Bozzaro, F. Siegert, and C.J. Weijer The role of the cortical cytoskeleton: F-actin crosslinking proteins protect against osmotic stress, ensure cell size, cell shape and motility, and contribute to phagocytosis and development J. Cell Sci. 109 1996 2679 2691
    • (1996) J. Cell Sci. , vol.109 , pp. 2679-2691
    • Rivero, F.1    Köppel, B.2    Peracino, B.3    Bozzaro, S.4    Siegert, F.5    Weijer, C.J.6
  • 3
    • 0142211212 scopus 로고    scopus 로고
    • Translocation of N-WASP by nuclear localization and export signals into the nucleus modulates expression of HSP90
    • S. Suetsugu, and T. Takenawa Translocation of N-WASP by nuclear localization and export signals into the nucleus modulates expression of HSP90 J. Biol. Chem. 278 2003 42515 42523
    • (2003) J. Biol. Chem. , vol.278 , pp. 42515-42523
    • Suetsugu, S.1    Takenawa, T.2
  • 5
    • 0032824776 scopus 로고    scopus 로고
    • Filamin is required for ring canal assembly and actin organization during Drosophila oogenesis
    • M.-G. Li, M. Serr, K. Edards, S. Ludmann, D. Yamamotot, and L.G. Tilney Filamin is required for ring canal assembly and actin organization during Drosophila oogenesis J. Cell Biol. 146 1999 1061 1074
    • (1999) J. Cell Biol. , vol.146 , pp. 1061-1074
    • Li, M.-G.1    Serr, M.2    Edards, K.3    Ludmann, S.4    Yamamotot, D.5    Tilney, L.G.6
  • 6
    • 0033523942 scopus 로고    scopus 로고
    • Drosophila filamin encoded by the cheerio locus is a component of ovarian ring canals
    • N. Sokol, and L. Cooley Drosophila filamin encoded by the cheerio locus is a component of ovarian ring canals Curr. Biol. 9 1999 1221 1230
    • (1999) Curr. Biol. , vol.9 , pp. 1221-1230
    • Sokol, N.1    Cooley, L.2
  • 7
    • 0021814573 scopus 로고
    • The filamins: Properties and functions
    • R.R. Weihing The filamins: properties and functions Can. J. Biochem. Cell Biol. 63 1985 397 413
    • (1985) Can. J. Biochem. Cell Biol. , vol.63 , pp. 397-413
    • Weihing, R.R.1
  • 8
    • 0028679744 scopus 로고
    • Actin-binding proteins 1: Spectrin superfamily
    • P. Sheterline Academic Press London
    • J. Hartwig Actin-binding proteins 1: spectrin superfamily P. Sheterline Protein Profile 1994 Academic Press London 711 778
    • (1994) Protein Profile , pp. 711-778
    • Hartwig, J.1
  • 10
    • 0031039776 scopus 로고    scopus 로고
    • The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold
    • P. Fucini, C. Renner, C. Herberhold, A.A. Noegel, and T.A. Holak The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold Nature Struct. Biol. 4 1997 223 230
    • (1997) Nature Struct. Biol. , vol.4 , pp. 223-230
    • Fucini, P.1    Renner, C.2    Herberhold, C.3    Noegel, A.A.4    Holak, T.A.5
  • 11
    • 0024335961 scopus 로고
    • The Dictyostelium gelation factor shares a putative actin binding site with alpha-actinins and dystrophin and also has a rod domain containing six 100-residue motifs that appear to have a cross-beta conformation
    • A.A. Noegel, S. Rapp, F. Lottspeich, M. Schleicher, and M. Stewart The Dictyostelium gelation factor shares a putative actin binding site with alpha-actinins and dystrophin and also has a rod domain containing six 100-residue motifs that appear to have a cross-beta conformation J. Cell. Biol. 109 1989 607 618
    • (1989) J. Cell. Biol. , vol.109 , pp. 607-618
    • Noegel, A.A.1    Rapp, S.2    Lottspeich, F.3    Schleicher, M.4    Stewart, M.5
  • 13
    • 0032832619 scopus 로고    scopus 로고
    • Structural basis for dimerization of the Dictyostelium gelation factor (ABP120) rod
    • A.J. McCoy, P. Fucini, A.A. Noegel, and M. Stewart Structural basis for dimerization of the Dictyostelium gelation factor (ABP120) rod Nature Struct. Biol. 6 1999 836 841
    • (1999) Nature Struct. Biol. , vol.6 , pp. 836-841
    • McCoy, A.J.1    Fucini, P.2    Noegel, A.A.3    Stewart, M.4
  • 14
    • 0031454113 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction characterization of a dimerizing fragment of the rod domain of the Dictyostelium gelation factor (ABP-120)
    • P. Fucini, A.J. McCoy, M. Gomez-Ortis, M. Schleicher, A.A. Noegel, and M. Stewart Crystallization and preliminary X-ray diffraction characterization of a dimerizing fragment of the rod domain of the Dictyostelium gelation factor (ABP-120) J. Struct. Biol. 120 1997 192 195
    • (1997) J. Struct. Biol. , vol.120 , pp. 192-195
    • Fucini, P.1    McCoy, A.J.2    Gomez-Ortis, M.3    Schleicher, M.4    Noegel, A.A.5    Stewart, M.6
  • 15
    • 0344132069 scopus 로고    scopus 로고
    • Molecular architecture of the rod domain of the Distyostelium gelation factor (ABP-120)
    • P. Fucini, B. Koppel, M. Schleicher, A. Lustig, T.A. Holak, and R. Muller Molecular architecture of the rod domain of the Distyostelium gelation factor (ABP-120) J. Mol. Biol. 291 1999 1017 1023
    • (1999) J. Mol. Biol. , vol.291 , pp. 1017-1023
    • Fucini, P.1    Koppel, B.2    Schleicher, M.3    Lustig, A.4    Holak, T.A.5    Muller, R.6
  • 16
    • 0037138385 scopus 로고    scopus 로고
    • The spectrin repeat: A structural platform for cytoskeletal protein assemblies
    • K. Djinovic-Carugo, M. Gautel, J. Ylanne, and P. Young The spectrin repeat: a structural platform for cytoskeletal protein assemblies FEBS Letters 513 2002 119 123
    • (2002) FEBS Letters , vol.513 , pp. 119-123
    • Djinovic-Carugo, K.1    Gautel, M.2    Ylanne, J.3    Young, P.4
  • 17
    • 0030740644 scopus 로고    scopus 로고
    • Flexibility and fine structure of smooth-muscle α-actinin
    • J. Winkler, H. Lunsdorf, and B.M. Jockusch Flexibility and fine structure of smooth-muscle α-actinin Eur. J. Biochem. 248 1997 193 199
    • (1997) Eur. J. Biochem. , vol.248 , pp. 193-199
    • Winkler, J.1    Lunsdorf, H.2    Jockusch, B.M.3
  • 19
    • 0036899405 scopus 로고    scopus 로고
    • Application of NMR in structural proteomics: Screening for proteins amenable to structural analysis
    • T. Rehm, R. Huber, and T.A. Holak Application of NMR in structural proteomics: screening for proteins amenable to structural analysis Structure 10 2002 1613 1618
    • (2002) Structure , vol.10 , pp. 1613-1618
    • Rehm, T.1    Huber, R.2    Holak, T.A.3
  • 20
    • 0034656331 scopus 로고    scopus 로고
    • Solution structure of PCP, a prototype for the peptidyl carrier domains of modular peptide synthetases
    • T. Weber, R. Baumgartner, C. Renner, M.A. Marahiel, and T.A. Holak Solution structure of PCP, a prototype for the peptidyl carrier domains of modular peptide synthetases Struct. Fold. Des. 8 2000 407 418
    • (2000) Struct. Fold. Des. , vol.8 , pp. 407-418
    • Weber, T.1    Baumgartner, R.2    Renner, C.3    Marahiel, M.A.4    Holak, T.A.5
  • 23
    • 0021143582 scopus 로고
    • Properties of the 120,000- and 95,000-dalton actin-binding proteins from Dictyostelium discoideum and their possible functions in assembling the cytoplasmic matrix
    • J. Condeelis, M. Vahey, J.M. Carboni, J. DeMey, and S. Ogihara Properties of the 120,000- and 95,000-dalton actin-binding proteins from Dictyostelium discoideum and their possible functions in assembling the cytoplasmic matrix J. Cell Biol. 99 1984 119s 126s
    • (1984) J. Cell Biol. , vol.99
    • Condeelis, J.1    Vahey, M.2    Carboni, J.M.3    Demey, J.4    Ogihara, S.5
  • 24
    • 0030050396 scopus 로고    scopus 로고
    • 2.0 Å crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region
    • D.J. Leahy, I. Aukhil, and H.P.2. Erickson 2.0 Å crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region Cell 84 1996 155 164
    • (1996) Cell , vol.84 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 25
  • 26
    • 0035839094 scopus 로고    scopus 로고
    • Modularity and homology: Modelling of the titin type I modules and their interfaces
    • P. Amodeo, F. Fraternali, A.M. Lesk, and A. Pastore Modularity and homology: modelling of the titin type I modules and their interfaces J. Mol. Biol. 31 2001 283 296
    • (2001) J. Mol. Biol. , vol.31 , pp. 283-296
    • Amodeo, P.1    Fraternali, F.2    Lesk, A.M.3    Pastore, A.4
  • 27
    • 0033538417 scopus 로고    scopus 로고
    • Modularity and homology: Modelling of the type II module family from titin
    • F. Fraternali, and A. Pastore Modularity and homology: modelling of the type II module family from titin J. Mol. Biol. 290 1999 581 593
    • (1999) J. Mol. Biol. , vol.290 , pp. 581-593
    • Fraternali, F.1    Pastore, A.2
  • 29
    • 0026727082 scopus 로고
    • A bacteriophage T7 RNA polymerase/promotor system for controlled exclusive expression of specific genes
    • S. Tabor, and C.C. Richardson A bacteriophage T7 RNA polymerase/promotor system for controlled exclusive expression of specific genes Biotechnology 24 1992 280 284
    • (1992) Biotechnology , vol.24 , pp. 280-284
    • Tabor, S.1    Richardson, C.C.2
  • 30
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • W. Kabsch Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants J. Appl. Crystallog. 26 1993 795 800
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 31
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallog. sect. D 50 1994 760 763
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 33
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density
    • D.E. McRee XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density J. Struct. Biol. 125 1999 156 165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.