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Volumn 39, Issue 2, 1998, Pages 402-411

Calcium induces a conformational change in the ligand binding domain of the low density lipoprotein receptor

Author keywords

Disulfide bonds; Divalent cations; Epidermal growth factor like repeats; Protein folding; Protein structure

Indexed keywords

LOW DENSITY LIPOPROTEIN RECEPTOR;

EID: 0031887229     PISSN: 00222275     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (26)

References (44)
  • 1
    • 0022549920 scopus 로고
    • A receptor-mediated pathway for cholesterol homeostasis
    • Brown, M. S., and J. L. Goldstein, 1986. A receptor-mediated pathway for cholesterol homeostasis. Science. 232: 34-47.
    • (1986) Science , vol.232 , pp. 34-47
    • Brown, M.S.1    Goldstein, J.L.2
  • 2
    • 0016241915 scopus 로고
    • Binding and degradation of low density lipoproteins by cultured human fibroblasts
    • Goldstein, J. L., and M. S. Brown. 1974. Binding and degradation of low density lipoproteins by cultured human fibroblasts. J. Biol. Chem. 249: 5153-5162.
    • (1974) J. Biol. Chem. , vol.249 , pp. 5153-5162
    • Goldstein, J.L.1    Brown, M.S.2
  • 3
    • 0022259920 scopus 로고
    • The LDL receptor gene: A mosaic of exons shared with different proteins
    • Südhof, T. C., J. L. Goldstein, M. S. Brown, and D. W. Russell. 1985. The LDL receptor gene: a mosaic of exons shared with different proteins. Science. 228: 815-822.
    • (1985) Science , vol.228 , pp. 815-822
    • Südhof, T.C.1    Goldstein, J.L.2    Brown, M.S.3    Russell, D.W.4
  • 7
    • 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., R. Q. Qian, D. W. McClure, and C. L. Maslen. 1994. Calcium binding, hydroxylation, and glycosylation of the precursor epidermal growth factor-like domains of fibrillin-1, the Marfan gene protein. J. Biol. Chem. 269: 26630-26634.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26630-26634
    • Glanville, R.W.1    Qian, R.Q.2    McClure, D.W.3    Maslen, C.L.4
  • 8
    • 0028931325 scopus 로고
    • The calcium binding properties and molecular organization of epidermal growth factor-like domains in human fibrillin-1
    • Handford, P., A. K. Downing, Z. Rao, D. R. Hewett, B. C. Sykes, and C. M. Kielty. 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
  • 9
    • 0025055089 scopus 로고
    • The first EGF-like domain from human factor IX contains a high-affinity calcium binding site
    • Handford, P. A., M. Baron, M. Mayhew, A. Willis, T. Beesley, G. G. Brownlee, and I. D. Campbell. 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
  • 10
    • 0024454718 scopus 로고
    • Calcium binding to the isolated β-hydroxyaspartic acid-containing epidermal growth factor-like domain of bovine factor X
    • Persson, F., M. Selander, S. Linse, T. Drakenberg, A-K. Öhlin, and J. Stenflo. 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, F.1    Selander, M.2    Linse, S.3    Drakenberg, T.4    Öhlin, A.-K.5    Stenflo, J.6
  • 11
    • 0023226782 scopus 로고
    • Calcium-dependent interaction between the epidermal growth factor precursor-like region of human protein C and a monuclonal antibody
    • Öhlin, A-K., and J. Stenflo. 1987. Calcium-dependent interaction between the epidermal growth factor precursor-like region of human protein C and a monuclonal antibody. J. Biol. Chem. 262: 13798-13804.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13798-13804
    • Öhlin, A.-K.1    Stenflo, J.2
  • 12
    • 0025166047 scopus 로고
    • Novel type of very high affinity calcium-binding sites in β-hydroxyasparagine-containing epidermal growth factor-like domains in vitamin K-dependent Protein S
    • Dahlbäck, B., B. Hildebrand, and S. Linse. 1990. Novel type of very high affinity calcium-binding sites in β-hydroxyasparagine-containing epidermal growth factor-like domains in vitamin K-dependent Protein S. J. Biol. Chem. 265: 18481-18489.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18481-18489
    • Dahlbäck, B.1    Hildebrand, B.2    Linse, S.3
  • 13
    • 0029020912 scopus 로고
    • Three-dimensional structure of a cysteine-rich repeat from the low-density lipoprotein receptor
    • Daly, N. L., M. J. Scanlon, J. T. Djordjevic, P. A. Kroon, and R. Smith. 1995. Three-dimensional structure of a cysteine-rich repeat from the low-density lipoprotein receptor. Proc. Natl. Acad. Sci. USA. 92: 6334-6338.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6334-6338
    • Daly, N.L.1    Scanlon, M.J.2    Djordjevic, J.T.3    Kroon, P.A.4    Smith, R.5
  • 14
    • 0028866813 scopus 로고
    • Three-dimensional structure of the second cysteine-rich repeat from the human low-density lipoprotein receptor
    • Daly, N. L., J. T. Djordjevic, P. A. Kroon, and R. Smith. 1995. Three-dimensional structure of the second cysteine-rich repeat from the human low-density lipoprotein receptor. Biochemistry. 34: 14474-14481.
    • (1995) Biochemistry , vol.34 , pp. 14474-14481
    • Daly, N.L.1    Djordjevic, J.T.2    Kroon, P.A.3    Smith, R.4
  • 15
    • 0029780956 scopus 로고    scopus 로고
    • Protein folding and calcium binding defects arising from familial hypercholesterolemia mutations of the LDL receptor
    • Blacklow, S. C., and P. S. Kim. 1996. Protein folding and calcium binding defects arising from familial hypercholesterolemia mutations of the LDL receptor. Nat. Struct. Biol. 3: 758-762.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 758-762
    • Blacklow, S.C.1    Kim, P.S.2
  • 16
    • 0030759357 scopus 로고    scopus 로고
    • Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module
    • Fass, D., S. Blacklow, P. S. Kim, and J. M. Berger. 1998. Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module. Nature. 388: 691-693.
    • (1998) Nature , vol.388 , pp. 691-693
    • Fass, D.1    Blacklow, S.2    Kim, P.S.3    Berger, J.M.4
  • 17
    • 0023750089 scopus 로고
    • Mutational analysis of the ligand binding domain of the low density lipoprotein receptor
    • Esser, V., L. E. Limbird, M. S. Brown, J. L. Goldstein and D. W. Russell. 1988. Mutational analysis of the ligand binding domain of the low density lipoprotein receptor. J. Biol. Chem. 263: 13282-13290.
    • (1988) J. Biol. Chem. , vol.263 , pp. 13282-13290
    • Esser, V.1    Limbird, L.E.2    Brown, M.S.3    Goldstein, J.L.4    Russell, D.W.5
  • 20
    • 0023140956 scopus 로고
    • The Lebanese allele at the low density lipoprotein receptor locus. Nonsense mutation produces truncated receptor that is retained in endoplasmic reticulum
    • Lehrman, M. A., W. J. Schneider, M. S. Brown, C. G. Davis, A. Elhammer, D. W. Russell, and J. L. Goldstein. 1987. The Lebanese allele at the low density lipoprotein receptor locus. Nonsense mutation produces truncated receptor that is retained in endoplasmic reticulum. J. Biol. Chem. 262: 401-410.
    • (1987) J. Biol. Chem. , vol.262 , pp. 401-410
    • Lehrman, M.A.1    Schneider, W.J.2    Brown, M.S.3    Davis, C.G.4    Elhammer, A.5    Russell, D.W.6    Goldstein, J.L.7
  • 21
    • 0030459796 scopus 로고    scopus 로고
    • Expression and characterization of a truncated, soluble, low-density lipoprotein receptor
    • Dirlam, K. A., D. G. Gretch, D. J. LaCount, S. L. Sturley, and A. D. Attie. 1996. Expression and characterization of a truncated, soluble, low-density lipoprotein receptor. Protein Expr. Purif. 8: 489-500.
    • (1996) Protein Expr. Purif. , vol.8 , pp. 489-500
    • Dirlam, K.A.1    Gretch, D.G.2    LaCount, D.J.3    Sturley, S.L.4    Attie, A.D.5
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0019551730 scopus 로고
    • "Western Blotting": Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A
    • Burnette, W. N. 1981. "Western Blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem. 112: 195-203.
    • (1981) Anal. Biochem. , vol.112 , pp. 195-203
    • Burnette, W.N.1
  • 24
    • 0019888656 scopus 로고
    • Monoclonal antibodies to the low density lipoprotein receptor as probes for study of receptor-mediated endocytosis and the genetics of familial hypercholesterolemia
    • Beisiegel, U., W. J. Schneider, J. L. Goldstein, R. G. W. Anderson, and M. S. Brown. 1981. Monoclonal antibodies to the low density lipoprotein receptor as probes for study of receptor-mediated endocytosis and the genetics of familial hypercholesterolemia. J. Biol. Chem. 256: 11923-11931.
    • (1981) J. Biol. Chem. , vol.256 , pp. 11923-11931
    • Beisiegel, U.1    Schneider, W.J.2    Goldstein, J.L.3    Anderson, R.G.W.4    Brown, M.S.5
  • 25
    • 0023665288 scopus 로고
    • Self-association of the low density lipoprotein receptor mediated by cytoptasmic domain
    • van Driel, I. R., C. G. Davis, J. L. Goldstein, and M. S. Brown. 1987. Self-association of the low density lipoprotein receptor mediated by cytoptasmic domain. J. Biol. Chem. 262: 16127-16134.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16127-16134
    • Van Driel, I.R.1    Davis, C.G.2    Goldstein, J.L.3    Brown, M.S.4
  • 26
    • 0021379023 scopus 로고
    • 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis
    • 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis. J. Biochem. (Toyko). 95: 511-519.
    • (1984) J. Biochem. (Toyko) , vol.95 , pp. 511-519
    • Maruyama, K.1    Mikawa, T.2    Ebashi, S.3
  • 27
  • 30
    • 0028822131 scopus 로고
    • Disulfide bridges of a cysteine-rich repeat of the LDL receptor ligand-binding domain
    • Bien, S., J. T. Djordjevic, N. L. Daly, R. Smith, and P. A. Kroon. 1995. Disulfide bridges of a cysteine-rich repeat of the LDL receptor ligand-binding domain. Biochemistry. 34: 13059-13065.
    • (1995) Biochemistry , vol.34 , pp. 13059-13065
    • Bien, S.1    Djordjevic, J.T.2    Daly, N.L.3    Smith, R.4    Kroon, P.A.5
  • 31
    • 0029133141 scopus 로고
    • Intracellular transport of proinsulin in pancreatic β-cells: Structural maturation probed by disulfide accessibility
    • Huang, X. F., and P. Arvan. 1995. Intracellular transport of proinsulin in pancreatic β-cells: structural maturation probed by disulfide accessibility. J. Biol. Chem. 270: 20417-20423.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20417-20423
    • Huang, X.F.1    Arvan, P.2
  • 32
    • 0029977996 scopus 로고    scopus 로고
    • Calcium binding properties of an epidermal growth factor-like domain pair from human fibrillin-1
    • Knott, V., A. K. Downing, C. M. Cardy, and P. Handford. 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
  • 33
    • 0023091262 scopus 로고
    • Acid-dependent ligand dissociation and recycling of LDL receptor mediated by growth factor homology region
    • Davis, C. G., J. L. Goldstein, T. C. Südhof, R. G. W. Anderson, D. W. Russell, and M. S. Brown, 1987. Acid-dependent ligand dissociation and recycling of LDL receptor mediated by growth factor homology region. Nature. 326: 760-765.
    • (1987) Nature , vol.326 , pp. 760-765
    • Davis, C.G.1    Goldstein, J.L.2    Südhof, T.C.3    Anderson, R.G.W.4    Russell, D.W.5    Brown, M.S.6
  • 34
    • 0025807804 scopus 로고
    • Thermal unfolding and aggregation of human complement protein G9: A differential scanning calorimetry study
    • Lohner, K., and A. F. Esser. 1991. Thermal unfolding and aggregation of human complement protein G9: a differential scanning calorimetry study. Biochemistry. 30: 6620-6625.
    • (1991) Biochemistry , vol.30 , pp. 6620-6625
    • Lohner, K.1    Esser, A.F.2
  • 36
    • 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., I. M. Jones, P. A. Handford, S. J. Walter, M. P. Esnouf, K. J. Smith, and G. G. Brownlee. 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
  • 38
    • 0023891841 scopus 로고
    • Human complement protein C9 is a calcium binding protein: Structural and functional implications
    • Thielens, N. M., K, Lohner, and A. F. Esser. 1988. Human complement protein C9 is a calcium binding protein: structural and functional implications. J. Biol. Chem. 263: 6665-6670.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6665-6670
    • Thielens, N.M.1    Lohner, K.2    Esser, A.F.3
  • 39
    • 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., V. Knott, J. M. Werner, C. M. Cardy, J. M. Campbell, and P. A. Handford. 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, J.M.3    Cardy, C.M.4    Campbell, J.M.5    Handford, P.A.6
  • 40
    • 0027141134 scopus 로고
    • The role of calcium in the organization of fibrillin microfibrils
    • Kielty, C. M., and C. A. Shuttleworth. 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
  • 41
    • 0031030185 scopus 로고    scopus 로고
    • Calcium stabilizes fibrillin-1 against proteolytic digestion
    • Reinhardt, D. P., R. N. Ono, and L. Y. Sakai. 1997. Calcium stabilizes fibrillin-1 against proteolytic digestion. J. Biol. Chem. 272: 1231-1236.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1231-1236
    • Reinhardt, D.P.1    Ono, R.N.2    Sakai, L.Y.3
  • 43
    • 0029240310 scopus 로고
    • Fibrillin domain folding and calcium binding: Significance to Marfan syndrome
    • Wu, Y-S., V. L. H. Bevilacqua, and J. M. Berg. 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
  • 44
    • 0013321009 scopus 로고
    • Familial hypercholesterolemia: Defective binding of lipoproteins to cultured fibroblasts associated with impaired regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity
    • Brown, M. S., and J. L. Goldstein. 1974. Familial hypercholesterolemia: defective binding of lipoproteins to cultured fibroblasts associated with impaired regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity. Proc. Natl. Acad. Sci. USA. 71: 788-792.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 788-792
    • Brown, M.S.1    Goldstein, J.L.2


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