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Volumn 16, Issue 22, 1997, Pages 6659-6666

Solution structure of the transforming growth factor β-binding protein-like module, a domain associated with matrix fibrils

Author keywords

8 cysteine domain; Human fibrillin 1; Marfan syndrome; NMR structure; TB domain

Indexed keywords

BINDING PROTEIN; FIBRILLIN; MUTANT PROTEIN; TRANSFORMING GROWTH FACTOR BETA;

EID: 0030781430     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (110)

References (51)
  • 1
    • 0029745110 scopus 로고    scopus 로고
    • Characterization of 4 novel fibrillin-1 (FBN1) mutations in Marfansyndrome
    • Ades, L.C., Haan, E.A., Colley, A.F. and Richaids, R.I. (1996) Characterization of 4 novel fibrillin-1 (FBN1) mutations in Marfansyndrome. J. Med. Genet., 33, 665-671.
    • (1996) J. Med. Genet. , vol.33 , pp. 665-671
    • Ades, L.C.1    Haan, E.A.2    Colley, A.F.3    Richaids, R.I.4
  • 2
    • 0027319447 scopus 로고
    • Identification of a cDNA for a human highmolecular-weight B-cell growth-factor
    • Ambrus, J.L. et al. (1993) Identification of a cDNA for a human highmolecular-weight B-cell growth-factor. Proc. Natl Acad. Sci. USA. 90, 6330-6334.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6330-6334
    • Ambrus, J.L.1
  • 3
    • 0006393051 scopus 로고
    • Two-dimensional spectroscopy: Application to nuclear magnetic resonance
    • Aue, W.P., Bartholdi, E. and Ernst, R.R. (1976) Two-dimensional spectroscopy: application to nuclear magnetic resonance. J. Chem. Phys., 64, 2229-2246.
    • (1976) J. Chem. Phys. , vol.64 , pp. 2229-2246
    • Aue, W.P.1    Bartholdi, E.2    Ernst, R.R.3
  • 4
    • 0026553672 scopus 로고
    • Prosite - A dictionary of sites and patterns in proteins
    • Bairoch, A. (1992) Prosite - a dictionary of sites and patterns in proteins. Nucleic Acids Res., 20, 2013-2018.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 2013-2018
    • Bairoch, A.1
  • 5
    • 0025303764 scopus 로고
    • Protein multiple sequence alignment and flexible pattern-matching
    • Barton, C.J. (1990) Protein multiple sequence alignment and flexible pattern-matching. Methods Enymol., 183, 403-428.
    • (1990) Methods Enymol. , vol.183 , pp. 403-428
    • Barton, C.J.1
  • 6
    • 5144233105 scopus 로고
    • MLHV-17-based two-dimensional homonuclcar magnetization transfer spectroscopy
    • Bax, A. and Davis, D.G. (1985) MLHV-17-based two-dimensional homonuclcar magnetization transfer spectroscopy. J. Magn. Resonance, 65, 355-360.
    • (1985) J. Magn. Resonance , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 7
    • 0029777325 scopus 로고    scopus 로고
    • Structure and distribution of modules in extracellular proteins
    • Bork, P., Downing, A.K., Kieffer, B. and Campbell, I.D. (1996) Structure and distribution of modules in extracellular proteins. Q. Rev. Biophys., 29, 119-167.
    • (1996) Q. Rev. Biophys. , vol.29 , pp. 119-167
    • Bork, P.1    Downing, A.K.2    Kieffer, B.3    Campbell, I.D.4
  • 8
    • 0344448273 scopus 로고
    • Coherence transfer by Isotropic mixing - Application to proton correlation spectroscopy
    • Braunschweiler, I., and Ernst, R.R. (1983) Coherence transfer by Isotropic mixing - application to proton correlation spectroscopy. J. Magn. Resonance, 53, 521-528.
    • (1983) J. Magn. Resonance , vol.53 , pp. 521-528
    • Braunschweiler, I.1    Ernst, R.R.2
  • 11
    • 1842336810 scopus 로고    scopus 로고
    • Marian database (second edition): Software and database for the analysis of mutations in the human FUN1 gene
    • Collod-Béroud, G. et al. (1997) Marian database (second edition): software and database for the analysis of mutations in the human FUN1 gene. Nucleic Acids Res., 25, 147-150.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 147-150
    • Collod-Béroud, G.1
  • 12
    • 0028885716 scopus 로고
    • Dual role for the latent transforming growth factor-β binding protein in storage of latent TGF-β in the extracellular matrix and as a structural matrix protein
    • Dallas, S.L., Miyazono, K., Skerry, T.M. Mundy, G.R. and Bonewald, L.F. (1995) Dual role for the latent transforming growth factor-β binding protein in storage of latent TGF-β in the extracellular matrix and as a structural matrix protein. J. Cell Biol., 131, 539-549.
    • (1995) J. Cell Biol. , vol.131 , pp. 539-549
    • Dallas, S.L.1    Miyazono, K.2    Skerry, T.M.3    Mundy, G.R.4    Bonewald, L.F.5
  • 13
    • 0028852659 scopus 로고
    • Mutations in the human gene for fibrillin-1 (FBN1) in the Marfan syndrome and related disorders
    • Dietz, H.C. and Pycritz, R.E. (1995) Mutations in the human gene for fibrillin-1 (FBN1) in the Marfan syndrome and related disorders. Hum. Mol. Genet., 4, 1799-1809.
    • (1995) Hum. Mol. Genet. , vol.4 , pp. 1799-1809
    • Dietz, H.C.1    Pycritz, R.E.2
  • 14
    • 0030000090 scopus 로고    scopus 로고
    • Solution structure of a pair of calcium-binding epidermal growth factor-like domains: Implications for the Marfan syndrome and other genetic disorders
    • Downing, A.K., Knott, V., Werner, M., Cardy, C.M., Campbell, I.D. and Handford, P.A. (1996) Solution structure of a pair of calcium-binding epidermal growth factor-like domains: Implications for the Marfan syndrome and other genetic disorders. Cell. 85, 597-605.
    • (1996) Cell , vol.85 , pp. 597-605
    • Downing, A.K.1    Knott, V.2    Werner, M.3    Cardy, C.M.4    Campbell, I.D.5    Handford, P.A.6
  • 15
    • 0025359788 scopus 로고
    • Nucleotide-sequence and genome organization of biologically active proviruses of the bovine immunodeficiency-like virus
    • Garvey, K.J., Oberste, M.S., Elser, J.E., Braun, M.J. and Gonda, M.A. (1990) Nucleotide-sequence and genome organization of biologically active proviruses of the bovine immunodeficiency-like virus. Virology. 175, 391-109.
    • (1990) Virology , vol.175 , pp. 391-1109
    • Garvey, K.J.1    Oberste, M.S.2    Elser, J.E.3    Braun, M.J.4    Gonda, M.A.5
  • 16
  • 17
    • 0028857166 scopus 로고
    • Bovine latent transforming growth factor β-binding protein 2: Molecular cloning. identification of tissue isoforms and immunolocalization to elaslin-associated microfibrils
    • Gibson, M.A., Hatzinikolas, G., Davis, E.C., Baker, E., Sutherland, G.R. and Mecham, R.P. (1995) Bovine latent transforming growth factor β-binding protein 2: Molecular cloning. identification of tissue isoforms and immunolocalization to elaslin-associated microfibrils. Mol. Cell. Biol., 15, 6932-6942.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6932-6942
    • Gibson, M.A.1    Hatzinikolas, G.2    Davis, E.C.3    Baker, E.4    Sutherland, G.R.5    Mecham, R.P.6
  • 18
    • 0029860747 scopus 로고    scopus 로고
    • Identification and characterization of an eight-cysteine repeat of the latent transforming growth factor-β binding protein-1 that mediates bonding to the latent transforming growth factor-β1
    • Gleizcs, P.-E., Beavis, R.C., Mazaeri, R., Shen, B. and Rifkin, D.B. (1996) Identification and characterization of an eight-cysteine repeat of the latent transforming growth factor-β binding protein-1 that mediates bonding to the latent transforming growth factor-β1. J. Biol. Chem., 271, 29891-29896.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29891-29896
    • Gleizcs, P.-E.1    Beavis, R.C.2    Mazaeri, R.3    Shen, B.4    Rifkin, D.B.5
  • 19
    • 0027569483 scopus 로고
    • Amino-acid type determination in the sequential assignment procedure of uniformly C-13/N-15-enriched proteins
    • Grzesiek, S. and Bax, A. (1993) Amino-acid type determination in the sequential assignment procedure of uniformly C-13/N-15-enriched proteins. J. Biomol. NMR. 3, 185-204.
    • (1993) J. Biomol. NMR , vol.3 , pp. 185-204
    • Grzesiek, S.1    Bax, A.2
  • 20
    • 0025055089 scopus 로고
    • The first EGF-like domain from human factor IX contains a high-affinity calcium binding site
    • Handford, P.A., Baron, M., Mayhew, M., Willis, A., Beesley, T., Brownlce, G.G. and Campbell, I.D. (1990) The first EGF-like domain from human factor IX contains a high-affinity calcium binding site. EMBO J., 9, 475-480.
    • (1990) EMBO J. , vol.9 , pp. 475-480
    • Handford, P.A.1    Baron, M.2    Mayhew, M.3    Willis, A.4    Beesley, T.5    Brownlce, G.G.6    Campbell, I.D.7
  • 21
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener, J., Meier, B.H., Bachmann, P. and Ernst, R.R. (1979) Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys., 71, 4546-4553.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 23
    • 45149137348 scopus 로고
    • New methods for the measurement of NHC-alpha-H coupling-constants in N-15-labeled proteins
    • Kay, L.E. and Bax.A. (1990) New methods for the measurement of NHC-alpha-H coupling-constants in N-15-labeled proteins. J. Magn. Resonance, 96, 110-126.
    • (1990) J. Magn. Resonance , vol.96 , pp. 110-126
    • Kay, L.E.1    Bax, A.2
  • 24
    • 0003026536 scopus 로고
    • Practical aspects of 3D heteronuclear NMR of proteins
    • Kay, L.E., Marion, D. and Bax, A. (1989) Practical aspects of 3D heteronuclear NMR of proteins. J. Magn. Resonance. 84, 72-84.
    • (1989) J. Magn. Resonance , vol.84 , pp. 72-84
    • Kay, L.E.1    Marion, D.2    Bax, A.3
  • 25
    • 0006925492 scopus 로고
    • Pure absorption gradient-enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay, L.E., Keifer, P. and Saarinen, T. (1992) Pure absorption gradient-enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc., 114, 10663-10665.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 26
    • 0029977996 scopus 로고    scopus 로고
    • Calcium binding properties of an epidermal growth factor-like domain pair
    • Knott, V., Downing, A.K., Cardy, C.M. and Handford, P. (1996) Calcium binding properties of an epidermal growth factor-like domain pair. J. Mol. Biol. 255, 22-27.
    • (1996) J. Mol. Biol. , vol.255 , pp. 22-27
    • Knott, V.1    Downing, A.K.2    Cardy, C.M.3    Handford, P.4
  • 27
    • 0025108122 scopus 로고
    • The murf 3 gene of Trypanosoma brucei contains multiple domains of extensive editing and is homologous to a subunit of NADH dehydrogenase
    • Koslowsky, D.J., Bhat, G.J., Perrollaz, A.L., Feagin, J.E. and Stuart, K. (1990) The murf 3 gene of Trypanosoma brucei contains multiple domains of extensive editing and is homologous to a subunit of NADH dehydrogenase. Cell. 62, 901-911.
    • (1990) Cell , vol.62 , pp. 901-911
    • Koslowsky, D.J.1    Bhat, G.J.2    Perrollaz, A.L.3    Feagin, J.E.4    Stuart, K.5
  • 28
    • 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
  • 29
    • 0029134243 scopus 로고
    • Mapping of human and murine genes for latent TGF-β binding protein2 (LTBP-2)
    • Li, X., Yin, W., Perez-Jurado, L., Bonadio, J. and Francke, U. (1995) Mapping of human and murine genes for latent TGF-β binding protein2 (LTBP-2). Mamm. Genome, 6, 42-45.
    • (1995) Mamm. Genome , vol.6 , pp. 42-45
    • Li, X.1    Yin, W.2    Perez-Jurado, L.3    Bonadio, J.4    Francke, U.5
  • 30
    • 49049150378 scopus 로고
    • 2-dimensional chemical-exchange and cross-relaxation spectroscopy of coupled nuclear spins
    • Macura, S., Huang, Y. Suter, D. and Ernst, R.R. (1981) 2-dimensional chemical-exchange and cross-relaxation spectroscopy of coupled nuclear spins. J. Magn. Resonance. 43, 259-281.
    • (1981) J. Magn. Resonance , vol.43 , pp. 259-281
    • Macura, S.1    Huang, Y.2    Suter, D.3    Ernst, R.R.4
  • 32
    • 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., 50, 869-873.
    • (1994) Acta Crystallogr. , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 33
    • 0028582165 scopus 로고
    • Identification and characterization of LTBP-2. a novel latent transforming growth factor-β binding protein
    • Moren, A. et al. (1994) Identification and characterization of LTBP-2. a novel latent transforming growth factor-β binding protein. J. Biol. Chem., 269, 32469-32478.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32469-32478
    • Moren, A.1
  • 34
    • 0028907436 scopus 로고
    • Calculation of protein structures with ambiguous distance restraints. Automated assignment of ambiguous NOE crosspeaks and disullide connectivities
    • Nilges, M. (1995) Calculation of protein structures with ambiguous distance restraints. Automated assignment of ambiguous NOE crosspeaks and disullide connectivities. J. Mol. Biol., 245, 645-660.
    • (1995) J. Mol. Biol. , vol.245 , pp. 645-660
    • Nilges, M.1
  • 35
    • 0023732144 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms
    • Nilges, M., Clore, G.M. and Gronenborn, A.M. (1988) Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. FEBS Lett., 239, 129-136.
    • (1988) FEBS Lett. , vol.239 , pp. 129-136
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 37
    • 0027313286 scopus 로고
    • Genomic organization of the sequence coding for fibrillin, the defective gene-product in Marfan-syndrome
    • Pereira, I., Dalessio, M., Ramirez, F., Lynch, J.R., Sykes, B., Pangilinan, T. and Bonadio J. (1993) Genomic organization of the sequence coding for fibrillin, the defective gene-product in Marfan-syndrome. Hum. Mol. Genel., 2, 961-968.
    • (1993) Hum. Mol. Genel. , vol.2 , pp. 961-968
    • Pereira, I.1    Dalessio, M.2    Ramirez, F.3    Lynch, J.R.4    Sykes, B.5    Pangilinan, T.6    Bonadio, J.7
  • 38
    • 0029867570 scopus 로고    scopus 로고
    • Cell-adhesion and integrin binding to recombinant human fibrillin-1
    • Pfaff, M., Reinhardt, D.P., Sakai, L.Y. and Timpl, R. (1996) Cell-adhesion and integrin binding to recombinant human fibrillin-1. FEBS Lett., 384, 247-250.
    • (1996) FEBS Lett. , vol.384 , pp. 247-250
    • Pfaff, M.1    Reinhardt, D.P.2    Sakai, L.Y.3    Timpl, R.4
  • 39
    • 0024296268 scopus 로고
    • Mcra and mcrb restriction phenotypes of some Escherichia coli strains and implications for gene cloning
    • Raleigh, E.A. et al. (1988) Mcra and mcrb restriction phenotypes of some Escherichia coli strains and implications for gene cloning. Nucleic Acids Res., 16, 1563-1575.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 1563-1575
    • Raleigh, E.A.1
  • 42
    • 0026743174 scopus 로고
    • Multiple protein-sequence alignment from tertiary structure comparison-assignment of global and residue confidence levels
    • Russell, R.B. and Barton, G.J. (1992) Multiple protein-sequence alignment from tertiary structure comparison-assignment of global and residue confidence levels. Proteins. 14, 309-323.
    • (1992) Proteins , vol.14 , pp. 309-323
    • Russell, R.B.1    Barton, G.J.2
  • 43
    • 0030058699 scopus 로고    scopus 로고
    • Association of the small latent transforming growth-factor-β with an 8-cysteine repeat of its binding-protein LTBP-1
    • Saharinen, J., Taipale, J. and Keski-OjaJ. (1996) Association of the small latent transforming growth-factor-β with an 8-cysteine repeat of its binding-protein LTBP-1. EMBO J., 15, 245-253.
    • (1996) EMBO J. , vol.15 , pp. 245-253
    • Saharinen, J.1    Taipale, J.2    Keski-Oja, J.3
  • 44
    • 0028929503 scopus 로고
    • Fibrillin: Monomers and microfibrils
    • Sakai, L.Y. and Keene, D.R. (1994) Fibrillin: Monomers and microfibrils. Methods Enzymol., 245, 29-52.
    • (1994) Methods Enzymol. , vol.245 , pp. 29-52
    • Sakai, L.Y.1    Keene, D.R.2
  • 45
    • 0026315446 scopus 로고
    • Purification and partial characterisation of fibrillin. a cysteine-rich structural component of connective-tissue microfibrils
    • Sakai, L.Y., Keene, D.R., Glanville, R.W. and Bachinger, H.P. (1991) Purification and partial characterisation of fibrillin. a cysteine-rich structural component of connective-tissue microfibrils. J. Biol. Chem., 266, 14763-14770.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14763-14770
    • Sakai, L.Y.1    Keene, D.R.2    Glanville, R.W.3    Bachinger, H.P.4
  • 46
    • 0029915120 scopus 로고    scopus 로고
    • Cell-type specific recognition of RGD- And non-RGU-containing cell binding domains in fihrillin-l
    • Sakamoto, H., Broekelmann, T., Cheresh, O.A., Ramirez, F., Rosenbloom, J. and Mecham, R.P. (1996) Cell-type specific recognition of RGD- and non-RGU-containing cell binding domains in fihrillin-l. J. Biol. Chem., 271, 4916-4922.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4916-4922
    • Sakamoto, H.1    Broekelmann, T.2    Cheresh, O.A.3    Ramirez, F.4    Rosenbloom, J.5    Mecham, R.P.6
  • 47
    • 0015860513 scopus 로고
    • Studies on the high-sulphur proteins of reduced merino wool: Amino acid sequence of protein SCMKB-IIIA3
    • Swart, I., S. and Haylett, T. (1973) Studies on the high-sulphur proteins of reduced merino wool: amino acid sequence of protein SCMKB-IIIA3. Biochem. J., 133, 641-654.
    • (1973) Biochem. J. , vol.133 , pp. 641-654
    • Swart, I.S.1    Haylett, T.2
  • 48
    • 0029813731 scopus 로고    scopus 로고
    • Latent transforming growth factor-β l and its binding protein arc components of extracellular matrix microfibrils
    • Taipale, J., Saharinen, J., Hedman, K. and Keski-Oja, J. (1996) Latent transforming growth factor-β l and its binding protein arc components of extracellular matrix microfibrils. J. Histochem. Cytochem., 44, 875-889.
    • (1996) J. Histochem. Cytochem. , vol.44 , pp. 875-889
    • Taipale, J.1    Saharinen, J.2    Hedman, K.3    Keski-Oja, J.4
  • 49
    • 0029783016 scopus 로고    scopus 로고
    • Morphology and biomechanics of the microfibrillar network of sea cucumber dermis
    • Thurmond, F.A. and Trotler, J.A. (1996) Morphology and biomechanics of the microfibrillar network of sea cucumber dermis. J. Exp. Biol., 199, 1817-1828.
    • (1996) J. Exp. Biol. , vol.199 , pp. 1817-1828
    • Thurmond, F.A.1    Trotler, J.A.2


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