메뉴 건너뛰기




Volumn 17, Issue 7, 1998, Pages 1883-1891

A distinct 14 residue site triggers coiled-coil formation in cortexillin I

Author keywords

Analytical ultracentrifugation; Autonomous helical folding unit; Circular dichroism spectroscopy; Electron microscopy; Heptad repeats

Indexed keywords

CORTEXILLIN I; PROTEIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 0032055747     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.7.1883     Document Type: Article
Times cited : (104)

References (56)
  • 1
    • 0030983330 scopus 로고    scopus 로고
    • A single amino acid can switch the oligomerization state of the ̈-helical coiled-coil domain of cartilage matrix protein
    • Beck,K., Gambee,J.E., Kamawal,A. and Bächinger, H.P. (1997) A single amino acid can switch the oligomerization state of the ̈-helical coiled-coil domain of cartilage matrix protein. EMBO J., 16, 3767-3777.
    • (1997) EMBO J. , vol.16 , pp. 3767-3777
    • Beck, K.1    Gambee, J.E.2    Kamawal, A.3    Bächinger, H.P.4
  • 2
    • 0029154811 scopus 로고
    • Native-like and structurally characterized designed α-helical bundles
    • Betz,S.F., Bryson,J.W. and DeGrado,W.F. (1995) Native-like and structurally characterized designed α-helical bundles. Curr. Opin. Struct. Biol., 5, 457-463.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 457-463
    • Betz, S.F.1    Bryson, J.W.2    DeGrado, W.F.3
  • 3
    • 0030465545 scopus 로고    scopus 로고
    • Native chick laminin-4 containing the β2 chain (s-laminin) promotes motor axon growth
    • Brandenberger,R., Kammerer,R.A., Engel,J. and Chiquet,M. (1996) Native chick laminin-4 containing the β2 chain (s-laminin) promotes motor axon growth. J. Cell Biol., 135, 1583-1592.
    • (1996) J. Cell Biol. , vol.135 , pp. 1583-1592
    • Brandenberger, R.1    Kammerer, R.A.2    Engel, J.3    Chiquet, M.4
  • 4
    • 0029957901 scopus 로고    scopus 로고
    • Heptad breaks in α-helical coiled coils: Stutters and stammers
    • Brown,J.H., Cohen,C. and Parry,D.A.D. (1996) Heptad breaks in α-helical coiled coils: stutters and stammers. Proteins, 26, 134-145.
    • (1996) Proteins , vol.26 , pp. 134-145
    • Brown, J.H.1    Cohen, C.2    Parry, D.A.D.3
  • 5
    • 0016169865 scopus 로고
    • Determination of the helix and β form of proteins in aqueous solution by circular dichroism
    • Chen,Y.-H., Yang,J.T. and Chau,K.H. (1974) Determination of the helix and β form of proteins in aqueous solution by circular dichroism. Biochemistry, 13, 3350-3359.
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.-H.1    Yang, J.T.2    Chau, K.H.3
  • 6
    • 0025272940 scopus 로고
    • α-Helical coiled-coils and bundles: How to design an α-helical protein
    • Cohen,C. and Parry,D.A.D. (1990) α-Helical coiled-coils and bundles: how to design an α-helical protein. Proteins, 7, 1-15.
    • (1990) Proteins , vol.7 , pp. 1-15
    • Cohen, C.1    Parry, D.A.D.2
  • 7
    • 0026028894 scopus 로고
    • Three-stranded ̈-fibrious proteins: The heptad repeat and its implications for structure
    • Conway,J.F. and Parry,D.A.D. (1991) Three-stranded ̈-fibrious proteins: the heptad repeat and its implications for structure. Int. J. Biol. Macromol., 13, 14-16.
    • (1991) Int. J. Biol. Macromol. , vol.13 , pp. 14-16
    • Conway, J.F.1    Parry, D.A.D.2
  • 8
    • 0000920828 scopus 로고
    • The packing of α-helices: Simple coiled-coils
    • Crick,F.H.C. (1953) The packing of α-helices: simple coiled-coils. Acta Crystallogr., 6, 689-697.
    • (1953) Acta Crystallogr. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 11
    • 0028936928 scopus 로고
    • Electron microscopy of extracellular matrix components
    • Engel,J. (1994) Electron microscopy of extracellular matrix components. Methods Enzymol., 245, 469-488.
    • (1994) Methods Enzymol. , vol.245 , pp. 469-488
    • Engel, J.1
  • 13
    • 16044367114 scopus 로고    scopus 로고
    • Cortexillins, major determinants of cell shape and size, are actin-bundling proteins with a parallel coiled-coil tail
    • Faix,J. et al. (1996) Cortexillins, major determinants of cell shape and size, are actin-bundling proteins with a parallel coiled-coil tail. Cell, 86, 631-642.
    • (1996) Cell , vol.86 , pp. 631-642
    • Faix, J.1
  • 14
    • 0000700060 scopus 로고
    • The coiled-coil model of α-keratin structure
    • Fraser,R.D.B., MacRae,T.P. and Miller,A. (1964) The coiled-coil model of α-keratin structure. J. Mol. Biol., 10, 147-156.
    • (1964) J. Mol. Biol. , vol.10 , pp. 147-156
    • Fraser, R.D.B.1    MacRae, T.P.2    Miller, A.3
  • 15
    • 0030963424 scopus 로고    scopus 로고
    • Fast events in protein folding: Relaxation dynamics of secondary and tertiary structure in native apomyoglobin
    • Gilmanshin,R., Williams,S., Callender,R.H., Woodruff,W.H. and Dyer,R.B. (1997) Fast events in protein folding: relaxation dynamics of secondary and tertiary structure in native apomyoglobin. Proc. Natl Acad. Sci. USA, 94, 3709-3713.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 3709-3713
    • Gilmanshin, R.1    Williams, S.2    Callender, R.H.3    Woodruff, W.H.4    Dyer, R.B.5
  • 16
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled-coils in GCN4 leucine zipper mutants
    • Harbury,P.B., Zhang,T., Kim,P.S. and Alber,T. (1993) A switch between two-, three-, and four-stranded coiled-coils in GCN4 leucine zipper mutants. Science, 262, 1401-1407.
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 17
    • 0027934571 scopus 로고
    • Crystal structure of an isoleucine-zipper trimer
    • Harbury,P.B., Kim,P.S. and Alber,T. (1994) Crystal structure of an isoleucine-zipper trimer. Nature, 371, 80-83.
    • (1994) Nature , vol.371 , pp. 80-83
    • Harbury, P.B.1    Kim, P.S.2    Alber, T.3
  • 18
    • 0030345054 scopus 로고    scopus 로고
    • De novo design of α-helical proteins: Basic research to medical applications
    • Hodges,R.S. (1996) De novo design of α-helical proteins: basic research to medical applications. Biochem. Cell Biol., 74, 133-154.
    • (1996) Biochem. Cell Biol. , vol.74 , pp. 133-154
    • Hodges, R.S.1
  • 19
    • 0030601794 scopus 로고    scopus 로고
    • Thermodynamic characterization of the coupled folding and association of heterodimeric coiled coils (leucine zippers)
    • Jelesarov,I, and Bosshard,H.R. (1996) Thermodynamic characterization of the coupled folding and association of heterodimeric coiled coils (leucine zippers). J. Mol. Biol., 263, 344-358.
    • (1996) J. Mol. Biol. , vol.263 , pp. 344-358
    • Jelesarov, I.1    Bosshard, H.R.2
  • 20
    • 0030935246 scopus 로고    scopus 로고
    • α-Helical coiled-coil oligomerization domains in extracellular proteins
    • Kammerer,R.A. (1997) α-Helical coiled-coil oligomerization domains in extracellular proteins. Matrix Biol., 15, 555-565.
    • (1997) Matrix Biol. , vol.15 , pp. 555-565
    • Kammerer, R.A.1
  • 21
    • 0029029181 scopus 로고
    • Selective chain recognition in the C-terminal α-helical coiled-coil region of laminin
    • Kammerer,R.A., Antonsson,P, Schulthess,T., Fauser,C. and Engel,J. (1995) Selective chain recognition in the C-terminal α-helical coiled-coil region of laminin. J. Mol. Biol., 250, 64-73.
    • (1995) J. Mol. Biol. , vol.250 , pp. 64-73
    • Kammerer, R.A.1    Antonsson, P.2    Schulthess, T.3    Fauser, C.4    Engel, J.5
  • 22
    • 0032562663 scopus 로고    scopus 로고
    • Tenascin-C hexabrachion assembly is a sequential two-step process initiated by coiled-coil α-helices
    • in press
    • Kammerer,R.A., Schulthess,T., Landwehr,R., Lustig,A. and Engel,J. (1998) Tenascin-C hexabrachion assembly is a sequential two-step process initiated by coiled-coil α-helices. J. Biol. Chem., in press.
    • (1998) J. Biol. Chem.
    • Kammerer, R.A.1    Schulthess, T.2    Landwehr, R.3    Lustig, A.4    Engel, J.5
  • 23
    • 0029038689 scopus 로고
    • Unfolding domains in smooth muscle myosin rod
    • King,L., Seidel,J.C. and Lehrer,S.S. (1995) Unfolding domains in smooth muscle myosin rod. Biochemistry, 34, 6770-6774.
    • (1995) Biochemistry , vol.34 , pp. 6770-6774
    • King, L.1    Seidel, J.C.2    Lehrer, S.S.3
  • 24
    • 0031027211 scopus 로고    scopus 로고
    • α-Helical protein assembly motifs
    • Kohn,W.D., Mant,C.T. and Hodges,R.S. (1997) α-Helical protein assembly motifs. J. Biol. Chem., 272, 2583-2586.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2583-2586
    • Kohn, W.D.1    Mant, C.T.2    Hodges, R.S.3
  • 25
    • 0017849306 scopus 로고
    • Effects of an interchain disulfide bond on tropomyosin structure: Intrinsic fluorescence and circular dichroism studies
    • Lehrer,S.S. (1978) Effects of an interchain disulfide bond on tropomyosin structure: intrinsic fluorescence and circular dichroism studies. J. Mol. Biol., 118, 209-226.
    • (1978) J. Mol. Biol. , vol.118 , pp. 209-226
    • Lehrer, S.S.1
  • 26
    • 0028306360 scopus 로고
    • Subdomain folding of the coiled coil leucine zipper from the bZIP transcriptional activator GCN4
    • Lumb,K.J., Carr,C.M. and Kim,P.S. (1994) Subdomain folding of the coiled coil leucine zipper from the bZIP transcriptional activator GCN4. Biochemistry, 33, 7361-7367.
    • (1994) Biochemistry , vol.33 , pp. 7361-7367
    • Lumb, K.J.1    Carr, C.M.2    Kim, P.S.3
  • 27
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: New structures and new functions
    • Lupas,A. (1996) Coiled coils: new structures and new functions. Trends Biochem, Sci., 21, 375-382.
    • (1996) Trends Biochem, Sci. , vol.21 , pp. 375-382
    • Lupas, A.1
  • 28
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas,A., Van Dyke,M. and Stock,J. (1991) Predicting coiled coils from protein sequences. Science, 252, 1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 29
    • 0029911261 scopus 로고    scopus 로고
    • The crystal structure of a five-stranded coiled coil in COMP: A prototype ion channel?
    • Malashkevich,V.N., Kammerer,R.A., Efimov,V.P., Schulthess,T. and Engel,J. (1996) The crystal structure of a five-stranded coiled coil in COMP: a prototype ion channel? Science, 274, 761-765.
    • (1996) Science , vol.274 , pp. 761-765
    • Malashkevich, V.N.1    Kammerer, R.A.2    Efimov, V.P.3    Schulthess, T.4    Engel, J.5
  • 31
    • 0026034515 scopus 로고
    • Modular organization of actin crosslinking proteins
    • Matsudaira,P. (1991) Modular organization of actin crosslinking proteins. Trends Biochem. Sci., 16, 87-92.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 87-92
    • Matsudaira, P.1
  • 32
    • 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
  • 33
    • 0026025936 scopus 로고
    • Kinetics of self-assembly of αα-tropomyosin coiled coils from unfolded chains
    • Mo,J., Holtzer,M.E. and Holtzer,A. (1991) Kinetics of self-assembly of αα-tropomyosin coiled coils from unfolded chains. Proc. Natl Acad. Sci USA, 88, 916-920.
    • (1991) Proc. Natl Acad. Sci USA , vol.88 , pp. 916-920
    • Mo, J.1    Holtzer, M.E.2    Holtzer, A.3
  • 34
    • 0026955797 scopus 로고
    • Kinetics of folding and unfolding of ββ-tropomyosin
    • Mo,J., Holtzer,M.E. and Holtzer,A. (1992) Kinetics of folding and unfolding of ββ-tropomyosin. Biopolymers, 32, 1581-1587.
    • (1992) Biopolymers , vol.32 , pp. 1581-1587
    • Mo, J.1    Holtzer, M.E.2    Holtzer, A.3
  • 35
    • 0028330850 scopus 로고
    • Electrostatic interactions control the parallel and antiparallel orientation of α-helical chains in double-stranded α-helical coiled-coils
    • Monera,O.D., Kay,C.M. and Hodges,R.S. (1994) Electrostatic interactions control the parallel and antiparallel orientation of α-helical chains in double-stranded α-helical coiled-coils. Biochemistry, 33, 3862-3871.
    • (1994) Biochemistry , vol.33 , pp. 3862-3871
    • Monera, O.D.1    Kay, C.M.2    Hodges, R.S.3
  • 36
    • 0024384644 scopus 로고
    • Preferential heterodimer formation by isolated leucine zippers from Fos and Jun
    • O'Shea,E.K., Rutkowski,R., Stafford III.W.F. and Kim,P.S. (1989) Preferential heterodimer formation by isolated leucine zippers from Fos and Jun. Science, 245, 646-648.
    • (1989) Science , vol.245 , pp. 646-648
    • O'Shea, E.K.1    Rutkowski, R.2    Stafford III, W.F.3    Kim, P.S.4
  • 37
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • O'Shea,E.K., Klemm,J.D., Kim,P.S. and 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
  • 38
    • 0026571898 scopus 로고
    • Mechanism of specificity in the Fos-Jun oncoprotein heterodimer
    • O'Shea,E.K., Rutkowski,R. and Kim,P.S. (1992) Mechanism of specificity in the Fos-Jun oncoprotein heterodimer. Cell, 68, 699-708.
    • (1992) Cell , vol.68 , pp. 699-708
    • O'Shea, E.K.1    Rutkowski, R.2    Kim, P.S.3
  • 39
    • 0029185909 scopus 로고
    • Design of α-helical peptides: Their role in protein folding and molecular biology
    • Parthasarathy,R., Chaturvedi,S. and Go,K. (1995) Design of α-helical peptides: their role in protein folding and molecular biology. Prog. Biophys. Mol. Biol., 64, 1-54.
    • (1995) Prog. Biophys. Mol. Biol. , vol.64 , pp. 1-54
    • Parthasarathy, R.1    Chaturvedi, S.2    Go, K.3
  • 40
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger,H. and von Jagow,G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem., 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 43
    • 0015463470 scopus 로고
    • Amino-acid sequence of rabbit skeletal tropomyosin and its coiled-coil structure
    • Sodek,J., Hodges,R.S., Smillie,L.B. and Jurasek,L. (1972) Amino-acid sequence of rabbit skeletal tropomyosin and its coiled-coil structure. Proc. Natl Acad. Sci. USA, 69, 3800-3804.
    • (1972) Proc. Natl Acad. Sci. USA , vol.69 , pp. 3800-3804
    • Sodek, J.1    Hodges, R.S.2    Smillie, L.B.3    Jurasek, L.4
  • 44
    • 0029990293 scopus 로고    scopus 로고
    • The role of helix formation in the folding of a fully α-helical coiled coil
    • Sosnick,T.R., Jackson,S., Wilk,R.R., Englander,S.W. and DeGrado,W.F. (1996) The role of helix formation in the folding of a fully α-helical coiled coil. Proteins, 24, 427-432.
    • (1996) Proteins , vol.24 , pp. 427-432
    • Sosnick, T.R.1    Jackson, S.2    Wilk, R.R.3    Englander, S.W.4    DeGrado, W.F.5
  • 45
    • 0013800421 scopus 로고
    • The interaction of naphtalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites
    • Stryer,L. (1965) The interaction of naphtalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites. J. Mol. Biol. 13, 482-495.
    • (1965) J. Mol. Biol. , vol.13 , pp. 482-495
    • Stryer, L.1
  • 46
    • 0028559469 scopus 로고
    • Effect of chain length on the formation and stability of synthetic α-helical coiled coils
    • Su,J.Y., Hodges,R.S. and Kay,C.M. (1994) Effect of chain length on the formation and stability of synthetic α-helical coiled coils. Biochemistry, 33, 15501-15510.
    • (1994) Biochemistry , vol.33 , pp. 15501-15510
    • Su, J.Y.1    Hodges, R.S.2    Kay, C.M.3
  • 47
    • 0027245801 scopus 로고
    • Thermodynamic characterization of the structural stability of the coiled-coil region of the bZIP transcription factor GCN4
    • Thompson,K.S., Vinson,C.R. and Freire,E. (1993) Thermodynamic characterization of the structural stability of the coiled-coil region of the bZIP transcription factor GCN4. Biochemistry, 32, 5491-5496.
    • (1993) Biochemistry , vol.32 , pp. 5491-5496
    • Thompson, K.S.1    Vinson, C.R.2    Freire, E.3
  • 48
    • 0030987241 scopus 로고    scopus 로고
    • Demonstration of coiled-coil interactions within the kinesin neck region using synthetic peptides
    • Tripet,B., Vale,R.D. and Hodges,R.S. (1997) Demonstration of coiled-coil interactions within the kinesin neck region using synthetic peptides. J. Biol. Chem., 272, 8946-8956.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8946-8956
    • Tripet, B.1    Vale, R.D.2    Hodges, R.S.3
  • 51
    • 0031012271 scopus 로고    scopus 로고
    • Very rapid, ionic strength-dependent association and folding of a heterodimeric leucine zipper
    • Wendt,H., Leder,L., Härmä.H., Jelesarov,I., Baici,A. and Bosshard,H.R. (1997) Very rapid, ionic strength-dependent association and folding of a heterodimeric leucine zipper. Biochemistry, 36, 204-213.
    • (1997) Biochemistry , vol.36 , pp. 204-213
    • Wendt, H.1    Leder, L.2    HärmäH3    Jelesarov, I.4    Baici, A.5    Bosshard, H.R.6
  • 53
    • 0014328849 scopus 로고
    • The lattice spacing of crystalline catalase as an internal standard of length in electron microscopy
    • Wrigley,N.G. (1968) The lattice spacing of crystalline catalase as an internal standard of length in electron microscopy. J. Ultrastruct. Res., 24, 454-464.
    • (1968) J. Ultrastruct. Res. , vol.24 , pp. 454-464
    • Wrigley, N.G.1
  • 54
    • 0026650710 scopus 로고
    • Synthetic model proteins: The relative contribution of leucine residues at the nonequivalent positions of the 3-4 hydrophobic repeat to the stability of the two-stranded α-helical coiled-coil
    • Zhou,N.E., Kay,C.M. and Hodges,R.S. (1992) Synthetic model proteins: the relative contribution of leucine residues at the nonequivalent positions of the 3-4 hydrophobic repeat to the stability of the two-stranded α-helical coiled-coil. Biochemistry, 31, 5739-5746.
    • (1992) Biochemistry , vol.31 , pp. 5739-5746
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3
  • 55
    • 0028364239 scopus 로고
    • The role of interhelical ionic interactions in controlling protein folding and stability
    • Zhou,N.E., Kay,C.M. and Hodges,R.S. (1994) The role of interhelical ionic interactions in controlling protein folding and stability. J. Mol. Biol., 237, 500-512.
    • (1994) J. Mol. Biol. , vol.237 , pp. 500-512
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3
  • 56
    • 0028783624 scopus 로고
    • Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopy
    • Zitzewitz,J.A., Bilsel,O., Luo,J., Jones,B.E. and Matthews,C.R. (1995) Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopy. Biochemistry, 34, 12812-12819.
    • (1995) Biochemistry , vol.34 , pp. 12812-12819
    • Zitzewitz, J.A.1    Bilsel, O.2    Luo, J.3    Jones, B.E.4    Matthews, C.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.