메뉴 건너뛰기




Volumn 85, Issue 4, 1996, Pages 597-605

Solution structure of a pair of calcium-binding epidermal growth factor-like domains: Implications for the Marfan syndrome and other genetic disorders

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR; FIBRILLIN; FIBULIN; LOW DENSITY LIPOPROTEIN RECEPTOR; THROMBOMODULIN;

EID: 0030000090     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81259-3     Document Type: Article
Times cited : (392)

References (53)
  • 1
    • 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
  • 2
    • 0026553672 scopus 로고
    • PROSITE: A dictionary of sites and patterns in proteins
    • Bairoch, A. (1992). PROSITE: a dictionary of sites and patterns in proteins. Nucl. Acids Res. 20 (suppl.), 2013-2018.
    • (1992) Nucl. Acids Res. , vol.20 , Issue.SUPPL. , pp. 2013-2018
    • Bairoch, A.1
  • 4
    • 0025303764 scopus 로고
    • Protein multiple sequence alignment and flexible pattern-matching
    • Barton, G.J. (1990). Protein multiple sequence alignment and flexible pattern-matching. Meth. Enzymol. 183, 403-428.
    • (1990) Meth. Enzymol. , vol.183 , pp. 403-428
    • Barton, G.J.1
  • 5
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A., and Davis, D.G. (1985). MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65, 355-360.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 7
    • 0028801352 scopus 로고
    • X-ray structure of clotting factor IXa: Active site and module structure related to Xase activity and hemophilia B
    • Brandstetter, H., Bauer, M., Huber, R., Lollar, P., and Bode, W. (1995). X-ray structure of clotting factor IXa: active site and module structure related to Xase activity and hemophilia B. Proc. Natl. Acad. Sci. USA 92, 9796-9800.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9796-9800
    • Brandstetter, H.1    Bauer, M.2    Huber, R.3    Lollar, P.4    Bode, W.5
  • 8
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Application to protein correlation spectroscopy
    • Braunschweiler, L.R., and Ernst, R.R. (1983). Coherence transfer by isotropic mixing: application to protein correlation spectroscopy. J. Magn. Reson. 53, 521-528.
    • (1983) J. Magn. Reson. , vol.53 , pp. 521-528
    • Braunschweiler, L.R.1    Ernst, R.R.2
  • 11
  • 12
    • 0025871254 scopus 로고
    • Structures of larger proteins in solution: Three- and four-dimensional heteronuclear NMR spectroscopy
    • Clore, G.M., and Gronenborn, A.M. (1991). Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy. Science 252, 1390-1399.
    • (1991) Science , vol.252 , pp. 1390-1399
    • Clore, G.M.1    Gronenborn, A.M.2
  • 13
    • 0027257818 scopus 로고
    • Fibrillin binds calcium and is coded by cDNAs that reveal a multidomain structure and alternatively spliced exons at the 5′ end
    • Corson, G.M., Chalberg, S.C., Dietz, H.C., Charbonneau, N.L., and Sakai, L.Y. (1993). Fibrillin binds calcium and is coded by cDNAs that reveal a multidomain structure and alternatively spliced exons at the 5′ end. Genomics 17, 476-484.
    • (1993) Genomics , vol.17 , pp. 476-484
    • Corson, G.M.1    Chalberg, S.C.2    Dietz, H.C.3    Charbonneau, N.L.4    Sakai, L.Y.5
  • 14
    • 0010662163 scopus 로고
    • Primary structure of bovine vitamin K-dependent protein S
    • Dahlbäck, B., Lundwall, A., and Stenflo, J. (1986). Primary structure of bovine vitamin K-dependent protein S. Proc. Natl. Acad. Sci. USA 83, 4199-4203.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4199-4203
    • Dahlbäck, B.1    Lundwall, A.2    Stenflo, J.3
  • 15
    • 0028852659 scopus 로고
    • Mutations in the human gene for fibrillin-1 (FBN1) in the Marfan syndrome and related disorders
    • Dietz, H.C., and Pyeritz, 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    Pyeritz, R.E.2
  • 16
    • 0025277746 scopus 로고
    • Molecular interactions between the protein products of the neurogenic loci Notch and Delta, two EGF-homologous genes in Drosophila
    • Fehon, R.G., Kooh, P.J., Rebay, I., Regan, C.L., Xu, T., Muskavitch, M.AT., and Artavanis-Tsakonas, S. (1990). Molecular interactions between the protein products of the neurogenic loci Notch and Delta, two EGF-homologous genes in Drosophila. Cell 61, 523-534.
    • (1990) Cell , vol.61 , pp. 523-534
    • Fehon, R.G.1    Kooh, P.J.2    Rebay, I.3    Regan, C.L.4    Xu, T.5    Muskavitch, M.A.T.6    Artavanis-Tsakonas, S.7
  • 17
    • 0028871033 scopus 로고
    • Identification of 15 different candidate causal point mutations and three polymorphisms in 19 patients with protein S deficiency using a scanning method for the analysis of the protein S active gene
    • Gandrille, S., Borgel, D., Eschwege-Gufflet, V., Aillaud, M., Dreyfus, M., Matheron, C., Gaussem, P., Abgrall, J.F., Jude, B., Sie, P., Toulon, P., and Aiach, M. (1995). Identification of 15 different candidate causal point mutations and three polymorphisms in 19 patients with protein S deficiency using a scanning method for the analysis of the protein S active gene. Blood 85, 130-138.
    • (1995) Blood , vol.85 , pp. 130-138
    • Gandrille, S.1    Borgel, D.2    Eschwege-Gufflet, V.3    Aillaud, M.4    Dreyfus, M.5    Matheron, C.6    Gaussem, P.7    Abgrall, J.F.8    Jude, B.9    Sie, P.10    Toulon, P.11    Aiach, M.12
  • 19
    • 0027959729 scopus 로고
    • Calcium binding, hydroxylation, and glycosylation of the precursor epidermal growth factor-like domains of fibrillin-1, the Marfan gene protein
    • Glanville, R.W., Quian, R-Q., McClure, D.W., and Maslen, C.L. (1994). Calcium binding, hydroxylation, and glycosylation of the precursor epidermal growth factor-like domains of fibrillin-1, the Marfan gene protein. J. Biol. Chem. 43, 26630-26634.
    • (1994) J. Biol. Chem. , vol.43 , pp. 26630-26634
    • Glanville, R.W.1    Quian, R.-Q.2    McClure, D.W.3    Maslen, C.L.4
  • 20
    • 0003648110 scopus 로고
    • University of Wisconsin, Madison, WI, USA
    • Genetics Computer Group. (1994). Program manual for the GCG package, version 8. University of Wisconsin, Madison, WI, USA.
    • (1994) Program Manual for the Gcg Package, Version 8
  • 21
    • 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., Brownlee, 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    Brownlee, G.G.6    Campbell, I.D.7
  • 23
    • 0028931325 scopus 로고
    • The calcium binding properties and molecular organization of epidermal growth factor-like domains in human fibrillin-1
    • Handford, P., Downing, A.K., Rao, Z., Hewett, D.R., Sykes, B.C., and Kielty, C.M. (1995). The calcium binding properties and molecular organization of epidermal growth factor-like domains in human fibrillin-1. J. Biol. Chem. 270, 6751-6756.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6751-6756
    • Handford, P.1    Downing, A.K.2    Rao, Z.3    Hewett, D.R.4    Sykes, B.C.5    Kielty, C.M.6
  • 24
    • 0027026881 scopus 로고
    • Molecular genetics of the LDL receptor gene in familial hypercholesterolemia
    • Hobbs, H.H., Brown, M.S., and Goldstein, J.L. (1992). Molecular genetics of the LDL receptor gene in familial hypercholesterolemia. Hum. Mutat. 1, 445-466.
    • (1992) Hum. Mutat. , vol.1 , pp. 445-466
    • Hobbs, H.H.1    Brown, M.S.2    Goldstein, J.L.3
  • 25
    • 0026662288 scopus 로고
    • Human epidermal growth factor: High resolution solution structure and comparison with human transforming growth factor α
    • Hommel, U., Harvey, T.S., Driscoll, P.C., and Campbell, I.D. (1992). Human epidermal growth factor: high resolution solution structure and comparison with human transforming growth factor α. J. Mol. Biol. 227, 271-282.
    • (1992) J. Mol. Biol. , vol.227 , pp. 271-282
    • Hommel, U.1    Harvey, T.S.2    Driscoll, P.C.3    Campbell, I.D.4
  • 26
    • 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
  • 27
    • 0003026536 scopus 로고
    • Practical aspects of 3D heteronuclear NMR of proteins
    • Kay, L.E., Marion, D., and Bax, A. (1989a). Practical aspects of 3D heteronuclear NMR of proteins. J. Magn. Reson. 83, 72-84.
    • (1989) J. Magn. Reson. , vol.83 , pp. 72-84
    • Kay, L.E.1    Marion, D.2    Bax, A.3
  • 28
    • 0024449503 scopus 로고
    • 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease
    • 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. Biochemistry 28, 8972-8979.
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 29
    • 45149137348 scopus 로고
    • New methods for the measurement of NH-C-α-H coupling constants in N-15 labeled proteins
    • Kay, L.E., and Bax, A. (1990). New methods for the measurement of NH-C-α-H coupling constants in N-15 labeled proteins. J. Magn. Reson. 86, 110-126.
    • (1990) J. Magn. Reson. , vol.86 , pp. 110-126
    • Kay, L.E.1    Bax, A.2
  • 30
    • 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
  • 31
    • 0026029066 scopus 로고
    • Extraction of extendable beaded structures and their identification as fibrillin-containing extracellular matrix microfibrils
    • Keene, D.R., Maddox, B.K., Kuo, H-J., Sakai, L.Y., and Glanville, R.W. (1991). Extraction of extendable beaded structures and their identification as fibrillin-containing extracellular matrix microfibrils. J. Histochem. Cytochem. 39, 441-449.
    • (1991) J. Histochem. Cytochem. , vol.39 , pp. 441-449
    • Keene, D.R.1    Maddox, B.K.2    Kuo, H.-J.3    Sakai, L.Y.4    Glanville, R.W.5
  • 32
    • 0027141134 scopus 로고
    • The role of calcium in the organization of fibrillin microfibrils
    • Kielty, C.M., and Shuttleworth, C.A. (1993). The role of calcium in the organization of fibrillin microfibrils. FEBS Lett. 336, 323-326.
    • (1993) FEBS Lett. , vol.336 , pp. 323-326
    • Kielty, C.M.1    Shuttleworth, C.A.2
  • 33
    • 0029977996 scopus 로고    scopus 로고
    • Calcium binding properties of an epidermal growth factor-like domain pair from human fibrillin-1
    • Knott, V., Downing, A.K., Cardy, C.M., and Handford, P. (1996). Calcium binding properties of an epidermal growth factor-like domain pair from human fibrillin-1. 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
  • 34
    • 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. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 35
    • 49049150378 scopus 로고
    • Two-dimensional chemical-exchange and cross-relaxation spectroscopy of coupled nuclear spins
    • Macura, S., Huang, Y., Suter, D., and Ernst, R.R. (1981). Two-dimensional chemical-exchange and cross-relaxation spectroscopy of coupled nuclear spins. J. Magn. Reson. 43, 259-281.
    • (1981) J. Magn. Reson. , vol.43 , pp. 259-281
    • Macura, S.1    Huang, Y.2    Suter, D.3    Ernst, R.R.4
  • 36
    • 0024849648 scopus 로고
    • Connective-tissue microfibrils: Isolation and characterization of 3 large pepsin-resistant domains of fibrillin
    • Maddox, B.K., Sakai, L.Y., Keene, D.R., and Glanville, R.W. (1989). Connective-tissue microfibrils: isolation and characterization of 3 large pepsin-resistant domains of fibrillin. J. Biol. Chem. 264, 21381-21385.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21381-21385
    • Maddox, B.K.1    Sakai, L.Y.2    Keene, D.R.3    Glanville, R.W.4
  • 38
    • 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 Cryst. 50, 869-873.
    • (1994) Acta Cryst. , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 39
    • 0028907436 scopus 로고
    • Calculation of protein structures with ambiguous distance restraints: Automated assignment of ambiguous NOE crosspeaks and disulphide connectivities
    • Nilges, M. (1995). Calculation of protein structures with ambiguous distance restraints: automated assignment of ambiguous NOE crosspeaks and disulphide connectivities. J. Mol. Biol. 245, 645-660.
    • (1995) J. Mol. Biol. , vol.245 , pp. 645-660
    • Nilges, M.1
  • 41
    • 0027313286 scopus 로고
    • Genomic organization of the sequence coding for fibrillin, the defective gene product in Marfan syndrome
    • Pereira, L., D'Alessio, 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. Genet. 2, 961-968.
    • (1993) Hum. Mol. Genet. , vol.2 , pp. 961-968
    • Pereira, L.1    D'Alessio, M.2    Ramirez, F.3    Lynch, J.R.4    Sykes, B.5    Pangilinan, T.6    Bonadio, J.7
  • 42
    • 0024454718 scopus 로고
    • Calcium binding to the isolated β-hydroxyaspartic acid-containing epidermal growth factor-like domain of bovine factor X
    • Persson, E., Selander, M., Linse, S., Drakenberg, T., Ohlin, A-K., and Stenflo, J. (1989). Calcium binding to the isolated β-hydroxyaspartic acid-containing epidermal growth factor-like domain of bovine factor X. J. Biol. Chem. 264, 16897-16904.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16897-16904
    • Persson, E.1    Selander, M.2    Linse, S.3    Drakenberg, T.4    Ohlin, A.-K.5    Stenflo, J.6
  • 44
    • 0024039803 scopus 로고
    • The role of β-hydroxyaspartate and adjacent carboxylate residues in the first EGF domain of human factor IX
    • Rees, D.J.G., Jones, I.M., Handford, P.A., Walter, S.J., Esnouf, M.P., Smith, K.J., and Brownlee, G.G. (1988). The role of β-hydroxyaspartate and adjacent carboxylate residues in the first EGF domain of human factor IX. EMBO J. 7, 2053-2061.
    • (1988) EMBO J. , vol.7 , pp. 2053-2061
    • Rees, D.J.G.1    Jones, I.M.2    Handford, P.A.3    Walter, S.J.4    Esnouf, M.P.5    Smith, K.J.6    Brownlee, G.G.7
  • 45
    • 0030058699 scopus 로고    scopus 로고
    • Association of the small latent transforming growth factor-β with an eight-cysteine repeat of its binding protein (LTBP-1)
    • Saharinen, J., Taipale, J., and Keski-Oja, J. (1996). Association of the small latent transforming growth factor-β with an eight-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
  • 46
    • 0026315446 scopus 로고
    • Purification and partial characterization 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 characterization 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
  • 47
    • 0028929503 scopus 로고
    • Fibrillin: Monomers and microfibrils
    • Sakai, L.Y., and Keene, D.R. (1994). Fibrillin: monomers and microfibrils. Meth. Enzymol. 245, 29-52.
    • (1994) Meth. Enzymol. , vol.245 , pp. 29-52
    • Sakai, L.Y.1    Keene, D.R.2
  • 49
    • 0026063331 scopus 로고
    • Structure-function relationships of epidermal growth factor modules in vitamin K-dependent clotting factors
    • Stenflo, J. (1991) Structure-function relationships of epidermal growth factor modules in vitamin K-dependent clotting factors. Blood 78, 1637-1651.
    • (1991) Blood , vol.78 , pp. 1637-1651
    • Stenflo, J.1
  • 50
    • 0028013177 scopus 로고
    • Improved sensitivity of profile searches through the use of sequence weights and gap excision
    • Thompson, J.D., Higgins, D.G., and Gibson, T.J. (1994). Improved sensitivity of profile searches through the use of sequence weights and gap excision. Comput. Appl. Biosci. 10, 19-29.
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 19-29
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 52
    • 0029240310 scopus 로고
    • Fibrillin domain folding and calcium binding: Significance to Marfan syndrome
    • Wu, Y.S., Bevilacqua, V.L.H., and Berg, J.M. (1995). Fibrillin domain folding and calcium binding: significance to Marfan syndrome. Chem. Biol. 2, 91-97.
    • (1995) Chem. Biol. , vol.2 , pp. 91-97
    • Wu, Y.S.1    Bevilacqua, V.L.H.2    Berg, J.M.3
  • 53
    • 0000517056 scopus 로고
    • Improved linear prediction for truncated signals of known phase
    • Zhu, G., and Bax, A. (1990). Improved linear prediction for truncated signals of known phase. J. Magn. Reson. 90, 405-410.
    • (1990) J. Magn. Reson. , vol.90 , pp. 405-410
    • Zhu, G.1    Bax, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.