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Volumn 8, Issue 3, 2000, Pages 223-230

The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges

Author keywords

Coiled coil; Cortexillin I; Dimerization; Protein design; Trigger site

Indexed keywords

LEUCINE ZIPPER PROTEIN; PROTEIN DERIVATIVE; PROTEIN SUBUNIT;

EID: 0034653908     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00100-3     Document Type: Article
Times cited : (114)

References (38)
  • 1
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: New structures and new functions
    • Lupas A. Coiled coils: new structures and new functions. Trends Biochem. Sci. 21:1996;375-382.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 375-382
    • Lupas, A.1
  • 2
    • 0030935246 scopus 로고    scopus 로고
    • Alpha-helical coiled-coil oligomerization domains in extracellular proteins
    • discussion 567-558.
    • Kammerer R.A. Alpha-helical coiled-coil oligomerization domains in extracellular proteins. Matrix Biol. 15:1997;555-565. discussion 567-558.
    • (1997) Matrix Biol. , vol.15 , pp. 555-565
    • Kammerer, R.A.1
  • 3
    • 0031027211 scopus 로고    scopus 로고
    • Alpha-helical protein assembly motifs
    • Kohn W.D., Mant C.T., Hodges R.S. Alpha-helical protein assembly motifs. J. Biol. Chem. 272:1997;2583-2586.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2583-2586
    • Kohn, W.D.1    Mant, C.T.2    Hodges, R.S.3
  • 4
    • 0025272940 scopus 로고
    • Alpha-helical coiled coils and bundles: How to design an alpha-helical protein
    • Cohen C., Parry D.A. Alpha-helical coiled coils and bundles: how to design an alpha-helical protein. Proteins. 7:1990;1-15.
    • (1990) Proteins , vol.7 , pp. 1-15
    • Cohen, C.1    Parry, D.A.2
  • 5
    • 0000920828 scopus 로고
    • The packing of α-helices: Simple coiled coils
    • Crick F.C.H. The packing of α-helices: simple coiled coils. Acta Crystallogr. 6:1953;689-697.
    • (1953) Acta Crystallogr. , vol.6 , pp. 689-697
    • Crick, F.C.H.1
  • 6
    • 0028894384 scopus 로고
    • Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA
    • Glover J.N., Harrison S.C. Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA. Nature. 373:1995;257-261.
    • (1995) Nature , vol.373 , pp. 257-261
    • Glover, J.N.1    Harrison, S.C.2
  • 7
    • 0023042847 scopus 로고
    • Tropomyosin crystal structure and muscle regulation
    • Phillips G.N. Jr., Fillers J.P., Cohen C. Tropomyosin crystal structure and muscle regulation. J. Mol. Biol. 192:1986;111-131.
    • (1986) J. Mol. Biol. , vol.192 , pp. 111-131
    • Phillips G.N., Jr.1    Fillers, J.P.2    Cohen, C.3
  • 8
    • 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., Gerisch G.et al. Cortexillins, major determinants of cell shape and size, are actin-bundling proteins with a parallel coiled-coil tail. Cell. 86:1996;631-642.
    • (1996) Cell , vol.86 , pp. 631-642
    • Faix, J.1    Gerisch, G.2
  • 10
    • 0030987241 scopus 로고    scopus 로고
    • Demonstration of coiled-coil interactions within the kinesin neck region using synthetic peptides. Implications for motor activity
    • Tripet B., Vale R.D., Hodges R.S. Demonstration of coiled-coil interactions within the kinesin neck region using synthetic peptides. Implications for motor activity. J. Biol. Chem. 272:1997;8946-8956.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8946-8956
    • Tripet, B.1    Vale, R.D.2    Hodges, R.S.3
  • 11
    • 0032055747 scopus 로고    scopus 로고
    • A distinct 14 residue site triggers coiled-coil formation in cortexillin I
    • Steinmetz M.O., Kammerer R.A.et al. A distinct 14 residue site triggers coiled-coil formation in cortexillin I. EMBO J. 17:1998;1883-1891.
    • (1998) EMBO J. , vol.17 , pp. 1883-1891
    • Steinmetz, M.O.1    Kammerer, R.A.2
  • 12
    • 0009670549 scopus 로고    scopus 로고
    • Structural properties of the myosin-II coiled-coil assembly domain
    • Turbedsky K., Pollard T.D. Structural properties of the myosin-II coiled-coil assembly domain. Mol. Biol. Cell. 9:1998;144a.
    • (1998) Mol. Biol. Cell , vol.9
    • Turbedsky, K.1    Pollard, T.D.2
  • 13
    • 0032506029 scopus 로고    scopus 로고
    • An autonomous folding unit mediates the assembly of two-stranded coiled coils
    • Kammerer R.A., Steinmetz M.O.et al. An autonomous folding unit mediates the assembly of two-stranded coiled coils. Proc. Natl. Acad. Sci. USA. 95:1998;13419-13424.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13419-13424
    • Kammerer, R.A.1    Steinmetz, M.O.2
  • 14
    • 0031657713 scopus 로고    scopus 로고
    • Crystallization and preliminary X-Ray diffraction analysis of the 190-A- long coiled-coil dimerization domain of the actin-bundling protein cortexillin I from Dictyostelium discoideum
    • Burkhard P., Kammerer R.A.et al. Crystallization and preliminary X-Ray diffraction analysis of the 190-A- long coiled-coil dimerization domain of the actin-bundling protein cortexillin I from Dictyostelium discoideum. J. Struct. Biol. 122:1998;293-296.
    • (1998) J. Struct. Biol. , vol.122 , pp. 293-296
    • Burkhard, P.1    Kammerer, R.A.2
  • 15
    • 0027934571 scopus 로고
    • Crystal structure of an isoleucine-zipper trimer
    • Harbury P.B., Kim P.S., Alber T. Crystal structure of an isoleucine-zipper trimer. Nature. 371:1994;80-83.
    • (1994) Nature , vol.371 , pp. 80-83
    • Harbury, P.B.1    Kim, P.S.2    Alber, T.3
  • 16
    • 0029083811 scopus 로고
    • Predicting oligomerization states of coiled coils
    • Woolfson D.N., Alber T. Predicting oligomerization states of coiled coils. Protein Sci. 4:1995;1596-1607.
    • (1995) Protein Sci. , vol.4 , pp. 1596-1607
    • Woolfson, D.N.1    Alber, T.2
  • 17
    • 0016774265 scopus 로고
    • Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure
    • McLachlan A.D., Stewart M. Tropomyosin coiled-coil interactions: evidence for an unstaggered structure. J. Mol. Biol. 98:1975;293-304.
    • (1975) J. Mol. Biol. , vol.98 , pp. 293-304
    • McLachlan, A.D.1    Stewart, M.2
  • 18
    • 0017379297 scopus 로고
    • Structure of alpha-keratin: Structural implication of the amino acid sequences of the type I and type II chain segments
    • Parry D.A., Crewther W.G., Fraser R.D., MacRae T.P. Structure of alpha-keratin: structural implication of the amino acid sequences of the type I and type II chain segments. J. Mol. Biol. 113:1977;449-454.
    • (1977) J. Mol. Biol. , vol.113 , pp. 449-454
    • Parry, D.A.1    Crewther, W.G.2    Fraser, R.D.3    MacRae, T.P.4
  • 19
    • 0029588555 scopus 로고
    • Complex salt bridges in proteins: Statistical analysis of structure and function
    • Musafia B., Buchner V., Arad D. Complex salt bridges in proteins: statistical analysis of structure and function. J. Mol. Biol. 254:1995;761-770.
    • (1995) J. Mol. Biol. , vol.254 , pp. 761-770
    • Musafia, B.1    Buchner, V.2    Arad, D.3
  • 20
    • 0029162070 scopus 로고
    • Understanding and increasing protein stability
    • Fagain C.O. Understanding and increasing protein stability. Biochim Biophys. Acta. 1252:1995;1-14.
    • (1995) Biochim Biophys. Acta , vol.1252 , pp. 1-14
    • Fagain, C.O.1
  • 21
    • 0031764838 scopus 로고    scopus 로고
    • Surface salt bridges stabilize the GCN4 leucine zipper
    • Spek E.J., Bui A.H., Lu M., Kallenbach N.R. Surface salt bridges stabilize the GCN4 leucine zipper. Protein Sci. 7:1998;2431-2437.
    • (1998) Protein Sci. , vol.7 , pp. 2431-2437
    • Spek, E.J.1    Bui, A.H.2    Lu, M.3    Kallenbach, N.R.4
  • 22
    • 0031471243 scopus 로고    scopus 로고
    • The crystal structure of dimeric kinesin and implications for microtubule-dependent motility
    • Kozielski F., Mandelkow E.et al. The crystal structure of dimeric kinesin and implications for microtubule-dependent motility. Cell. 91:1997;985-994.
    • (1997) Cell , vol.91 , pp. 985-994
    • Kozielski, F.1    Mandelkow, E.2
  • 23
    • 0032493843 scopus 로고    scopus 로고
    • Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper
    • Lavigne P., Crump M.P, Gagne S.M., Hodges R.S., Kay C.M., Sykes B.D. Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper. J. Mol. Biol. 281:1998;165-181.
    • (1998) J. Mol. Biol. , vol.281 , pp. 165-181
    • Lavigne, P.1    Crump, M.P.2    Gagne, S.M.3    Hodges, R.S.4    Kay, C.M.5    Sykes, B.D.6
  • 24
    • 0029563395 scopus 로고
    • Preferential heterodimeric parallel coiled-coil formation by synthetic Max and c-Myc leucine zippers: A description of putative electrostatic interactions responsible for the specificity of heterodimerization
    • Lavigne P., Kay C.M.et al. Preferential heterodimeric parallel coiled-coil formation by synthetic Max and c-Myc leucine zippers: a description of putative electrostatic interactions responsible for the specificity of heterodimerization. J. Mol. Biol. 254:1995;505-520.
    • (1995) J. Mol. Biol. , vol.254 , pp. 505-520
    • Lavigne, P.1    Kay, C.M.2
  • 25
    • 0027949381 scopus 로고
    • The net energetic contribution of interhelical electrostatic attractions to coiled-coil stability
    • Zhou N.E., Kay C.M., Hodges R.S. The net energetic contribution of interhelical electrostatic attractions to coiled-coil stability. Protein Eng. 7:1994;1365-1372.
    • (1994) Protein Eng. , vol.7 , pp. 1365-1372
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3
  • 26
    • 0029030233 scopus 로고
    • Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper
    • Lumb K.J., Kim P.S. Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper. Science. 268:1995;436-439.
    • (1995) Science , vol.268 , pp. 436-439
    • Lumb, K.J.1    Kim, P.S.2
  • 27
    • 0029926150 scopus 로고    scopus 로고
    • Interhelical salt bridges, coiled-coil stability, and specificity of dimerization
    • Lavigne P., Soennichsen F.D., Kay C.M., Hodges R.S. Interhelical salt bridges, coiled-coil stability, and specificity of dimerization. Science. 271:1996;1136-1137.
    • (1996) Science , vol.271 , pp. 1136-1137
    • Lavigne, P.1    Soennichsen, F.D.2    Kay, C.M.3    Hodges, R.S.4
  • 28
    • 0029926150 scopus 로고    scopus 로고
    • Interhelical salt bridges, coiled-coil stability, and specificity of dimerization
    • Lumb K.J., Kim P.S. Interhelical salt bridges, coiled-coil stability, and specificity of dimerization. Science. 271:1996;1137-1138.
    • (1996) Science , vol.271 , pp. 1137-1138
    • Lumb, K.J.1    Kim, P.S.2
  • 29
    • 0030345054 scopus 로고    scopus 로고
    • Boehringer Mannheim award lecture 1995. La conference Boehringer Mannheim 1995. De novo design of alpha-helical proteins: Basic research to medical applications
    • Hodges R.S. Boehringer Mannheim award lecture 1995. La conference Boehringer Mannheim 1995. De novo design of alpha-helical proteins: basic research to medical applications. Biochem. Cell Biol. 74:1996;133-154.
    • (1996) Biochem. Cell Biol. , vol.74 , pp. 133-154
    • Hodges, R.S.1
  • 30
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • J.C.W. Carter. San Diego: Academic Press
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Carter J.C.W. Methods in Enzymology, vol. 277 Part A. 1997;Academic Press, San Diego.
    • (1997) Methods in Enzymology, Vol. 277 Part a
    • Otwinowski, Z.1    Minor, W.2
  • 32
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 33
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • J.C.W. Carter. San Diego: Academic Press
    • De La Fortelle E., Bricogne G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Carter J.C.W. Methods Enzymol., vol. 277 Part A. 1997;Academic Press, San Diego.
    • (1997) Methods Enzymol., Vol. 277 Part a
    • De La Fortelle, E.1    Bricogne, G.2
  • 34
    • 84945092441 scopus 로고
    • The use of Sayre's equation with solvent flattening and histogram matching for phase extension and refinement of protein structures
    • Zhang K.Y.J., Main P. The use of Sayre's equation with solvent flattening and histogram matching for phase extension and refinement of protein structures. Acta Crystallogr. A. 46:1990;377-381.
    • (1990) Acta Crystallogr. a , vol.46 , pp. 377-381
    • Zhang, K.Y.J.1    Main, P.2
  • 35
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;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
  • 36
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger A.T., Warren G.L.et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54:1998;905-921.
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 905-921
    • Brünger, A.T.1    Warren, G.L.2
  • 37
    • 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., Alber T. A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science. 262:1993;1401-1407.
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 38
    • 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., Alber T. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science. 254:1991;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


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