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Volumn 289, Issue 4, 1999, Pages 1109-1118

The transferrin receptor binding site on HFE, the class I MHC-related protein mutated in hereditary hemochromatosis

Author keywords

Class I MHC homolog; Functional epitope; Iron overload; pH dependent affinity; Surface plasmon resonance

Indexed keywords

MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; TRANSFERRIN RECEPTOR;

EID: 0033020518     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2842     Document Type: Article
Times cited : (84)

References (40)
  • 1
    • 0032530340 scopus 로고    scopus 로고
    • Iron is hot: An update on the pathophysiology of hemochromatosis
    • Andrews N. C., Levy J. E. Iron is hot: an update on the pathophysiology of hemochromatosis. Blood. 92:1998;1845-1851.
    • (1998) Blood , vol.92 , pp. 1845-1851
    • Andrews, N.C.1    Levy, J.E.2
  • 2
    • 0000007950 scopus 로고
    • The use of vectors based on gene amplification for the expression of cloned genes in mammalian cells
    • D. M. Glover. Oxford: IRL Press
    • Bebbington C. R., Hentschel C. C. G. The use of vectors based on gene amplification for the expression of cloned genes in mammalian cells. Glover D. M. DNA Cloning: A Practical Approach. 1987;163-188 IRL Press, Oxford.
    • (1987) DNa Cloning: A Practical Approach , pp. 163-188
    • Bebbington, C.R.1    Hentschel, C.C.G.2
  • 4
    • 0028089908 scopus 로고
    • Crystal structure of the complex of rat neonatal Fc receptor with Fc
    • Burmeister W. P., Huber A. H., Bjorkman P. J. Crystal structure of the complex of rat neonatal Fc receptor with Fc. Nature. 372:1994;379-383.
    • (1994) Nature , vol.372 , pp. 379-383
    • Burmeister, W.P.1    Huber, A.H.2    Bjorkman, P.J.3
  • 6
    • 0027132097 scopus 로고
    • HLA-C is the inhibitory ligand that determines domain resistance to lysis by NK1- And NK2-specific natural killer cells
    • Colonna M., Borsellino G., Falco M., Ferrara G. B., Strominger J. L. HLA-C is the inhibitory ligand that determines domain resistance to lysis by NK1- and NK2-specific natural killer cells. Proc. Natl Acad. Sci. USA. 90:1993;12000-12004.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 12000-12004
    • Colonna, M.1    Borsellino, G.2    Falco, M.3    Ferrara, G.B.4    Strominger, J.L.5
  • 7
    • 0031296864 scopus 로고    scopus 로고
    • Iron, HFE, and hemochromatosis update
    • Cuthbert J. A. Iron, HFE, and hemochromatosis update. J. Invest. Med. 45:1997;518-529.
    • (1997) J. Invest. Med. , vol.45 , pp. 518-529
    • Cuthbert, J.A.1
  • 8
    • 0029764534 scopus 로고    scopus 로고
    • A mutational analysis of the binding of two different proteins to the same antibody
    • Dall'Acqua W., Goldman E. R., Eisenstein E., Mariuzza R. A. A mutational analysis of the binding of two different proteins to the same antibody. Biochemistry. 35:1996;9667-9676.
    • (1996) Biochemistry , vol.35 , pp. 9667-9676
    • Dall'Acqua, W.1    Goldman, E.R.2    Eisenstein, E.3    Mariuzza, R.A.4
  • 9
    • 0031941594 scopus 로고    scopus 로고
    • Mechanism of acidification of the trans-Golgi network (TGN)- In situ measurements of pH using retrieval of TGN38 and furin from the cell surface
    • DeMaurex N., Furuya W., Dsouza S., Bonifacino J. S., Grinstein S. Mechanism of acidification of the trans-Golgi network (TGN)- in situ measurements of pH using retrieval of TGN38 and furin from the cell surface. J. Biol. Chem. 273:1998;2044-2051.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2044-2051
    • Demaurex, N.1    Furuya, W.2    Dsouza, S.3    Bonifacino, J.S.4    Grinstein, S.5
  • 10
    • 0027074320 scopus 로고
    • Thermal stability comparison of purified empty and peptide filled forms of a class I MHC molecule
    • Fahnestock M. L., Tamir I., Narhi L., Bjorkman P. J. Thermal stability comparison of purified empty and peptide filled forms of a class I MHC molecule. Science. 258:1992;1658-1662.
    • (1992) Science , vol.258 , pp. 1658-1662
    • Fahnestock, M.L.1    Tamir, I.2    Narhi, L.3    Bjorkman, P.J.4
  • 16
    • 0026569633 scopus 로고
    • Expression and crystallization of a soluble and functional form of an Fc receptor related to class I histocompatibility molecules
    • Gastinel L. N., Simister N. E., Bjorkman P. J. Expression and crystallization of a soluble and functional form of an Fc receptor related to class I histocompatibility molecules. Proc. Natl Acad. Sci. USA. 89:1992;638-642.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 638-642
    • Gastinel, L.N.1    Simister, N.E.2    Bjorkman, P.J.3
  • 17
    • 0032555601 scopus 로고    scopus 로고
    • Co-trafficking of HFE, a non-classical major histocompatibility complex class I protein, with the transferrin receptor implies a role in intracellular iron regulation
    • Gross C. N., Irrinki A., Feder J. N., Enns C. A. Co-trafficking of HFE, a non-classical major histocompatibility complex class I protein, with the transferrin receptor implies a role in intracellular iron regulation. J. Biol. Chem. 273:1998;22068-22074.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22068-22074
    • Gross, C.N.1    Irrinki, A.2    Feder, J.N.3    Enns, C.A.4
  • 18
    • 0031550247 scopus 로고    scopus 로고
    • Identification of a mouse homolog for the human hereditary haemochromatosis candidate gene
    • Hashimoto K., Hirai M., Kurosawa Y. Identification of a mouse homolog for the human hereditary haemochromatosis candidate gene. Biochem. Biophys. Res. Commun. 230:1997;35-39.
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 35-39
    • Hashimoto, K.1    Hirai, M.2    Kurosawa, Y.3
  • 19
    • 0026409862 scopus 로고
    • Perspectives on non-heme iron protein chemistry
    • Howard J. B., Rees D. C. Perspectives on non-heme iron protein chemistry. Advan. Protein Chem. 42:1991;199-280.
    • (1991) Advan. Protein Chem. , vol.42 , pp. 199-280
    • Howard, J.B.1    Rees, D.C.2
  • 20
    • 0030993535 scopus 로고    scopus 로고
    • Finally! The brambell receptor (FcRB). Mediator of transmission of immunity and protection from catabolism for IgG
    • Junghans R. P. Finally! The brambell receptor (FcRB). Mediator of transmission of immunity and protection from catabolism for IgG. Immunol. Res. 16:1997;29-57.
    • (1997) Immunol. Res. , vol.16 , pp. 29-57
    • Junghans, R.P.1
  • 21
    • 0342813129 scopus 로고    scopus 로고
    • Experimental design for kinetic analysis of protein-protein interactions with surface plasmon resonance biosensors
    • Karlsson R., Fält A. Experimental design for kinetic analysis of protein-protein interactions with surface plasmon resonance biosensors. J. Immunol. Methods. 200:1997;121-133.
    • (1997) J. Immunol. Methods , vol.200 , pp. 121-133
    • Karlsson, R.1    Fält, A.2
  • 22
    • 0027228495 scopus 로고
    • Thermodynamic analysis of an antibody functional epitope
    • Kelley R. F., O'Connell M. P. Thermodynamic analysis of an antibody functional epitope. Biochemistry. 32:1993;6828-6835.
    • (1993) Biochemistry , vol.32 , pp. 6828-6835
    • Kelley, R.F.1    O'Connell, M.P.2
  • 23
    • 0023613953 scopus 로고
    • Rapid and efficient site directed mutagenesis without phenotypic selection
    • Kunkel T. A., Roberts J. D., Zakour R. A. Rapid and efficient site directed mutagenesis without phenotypic selection. Methods Enzymol. 154:1987;367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 24
    • 0032478524 scopus 로고    scopus 로고
    • Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor
    • Lebrón J. A., Bennett M. J., Vaughn D. E., Chirino A. J., Snow P. M., Mintier G. A., Feder J. N., Bjorkman P. J. Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor. Cell. 93:1998;111-123.
    • (1998) Cell , vol.93 , pp. 111-123
    • Lebrón, J.A.1    Bennett, M.J.2    Vaughn, D.E.3    Chirino, A.J.4    Snow, P.M.5    Mintier, G.A.6    Feder, J.N.7    Bjorkman, P.J.8
  • 25
    • 0032898068 scopus 로고    scopus 로고
    • Tolerization of adult mice to immunodominant proteins before monoclonal antibody production
    • Lebrón J. A., Shen H., Bjorkman P. J., Ou S. Tolerization of adult mice to immunodominant proteins before monoclonal antibody production. J. Immunol. Methods. 222:1999;59-63.
    • (1999) J. Immunol. Methods , vol.222 , pp. 59-63
    • Lebrón, J.A.1    Shen, H.2    Bjorkman, P.J.3    Ou, S.4
  • 26
    • 0032499784 scopus 로고    scopus 로고
    • Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins
    • Llopid J., McCaffery J. M., Miyawaki A., Farquhar M. G., Tsien R. Y. Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins. Proc. Natl Acad. Sci. USA. 95:1998;6803-6808.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6803-6808
    • Llopid, J.1    McCaffery, J.M.2    Miyawaki, A.3    Farquhar, M.G.4    Tsien, R.Y.5
  • 27
    • 0028943275 scopus 로고
    • The three dimensional structure of peptide-MHC complexes
    • Madden D. R. The three dimensional structure of peptide-MHC complexes. Annu. Rev. Immunol. 13:1995;587-622.
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 587-622
    • Madden, D.R.1
  • 28
    • 0027916175 scopus 로고
    • Biospecific interaction analysis using biosensor technology
    • Malmqvist M. Biospecific interaction analysis using biosensor technology. Nature. 361:1993;186-187.
    • (1993) Nature , vol.361 , pp. 186-187
    • Malmqvist, M.1
  • 31
    • 0031567095 scopus 로고    scopus 로고
    • The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells
    • Richardson D. R., Ponka P. The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells. Biochim. Biophys. Acta. 1331:1997;1-40.
    • (1997) Biochim. Biophys. Acta , vol.1331 , pp. 1-40
    • Richardson, D.R.1    Ponka, P.2
  • 32
    • 0025339432 scopus 로고
    • Regulation of insulin receptor functions by a peptide derived from a major histocompatibility complex class I antigen
    • Stagsted J., Reaven G. M., Hansen T., Goldstein A., Olsson L. Regulation of insulin receptor functions by a peptide derived from a major histocompatibility complex class I antigen. Cell. 62:1990;297-307.
    • (1990) Cell , vol.62 , pp. 297-307
    • Stagsted, J.1    Reaven, G.M.2    Hansen, T.3    Goldstein, A.4    Olsson, L.5
  • 33
    • 0027237516 scopus 로고
    • Amino acid residues essential for biological activity of a peptide derived from a major histocompatibility complex class I antigen
    • Stagsted J., Mapelli C., Meyers C., Matthews B. W., Anfinsen C. B., Goldstein A., Olsson L. Amino acid residues essential for biological activity of a peptide derived from a major histocompatibility complex class I antigen. Proc. Natl Acad. Sci. USA. 90:1993;7686-7690.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 7686-7690
    • Stagsted, J.1    Mapelli, C.2    Meyers, C.3    Matthews, B.W.4    Anfinsen, C.B.5    Goldstein, A.6    Olsson, L.7
  • 34
    • 0029098489 scopus 로고
    • Role of Tyr residues in the contact region of anti-lysozyme monoclonal antibody HyHEL10 for antigen binding
    • Tsumoto K., Ogasahara K., Ueda Y., Watanabe K., Yutani K., Kumagai I. Role of Tyr residues in the contact region of anti-lysozyme monoclonal antibody HyHEL10 for antigen binding. J. Biol. Chem. 270:1995;18551-18557.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18551-18557
    • Tsumoto, K.1    Ogasahara, K.2    Ueda, Y.3    Watanabe, K.4    Yutani, K.5    Kumagai, I.6
  • 35
    • 0030806484 scopus 로고    scopus 로고
    • High affinity binding of the neonatal Fc receptor to its IgG ligand requires receptor immobilization
    • Vaughn D. E., Bjorkman P. J. High affinity binding of the neonatal Fc receptor to its IgG ligand requires receptor immobilization. Biochemistry. 36:1997;9374-9380.
    • (1997) Biochemistry , vol.36 , pp. 9374-9380
    • Vaughn, D.E.1    Bjorkman, P.J.2
  • 36
    • 0032518373 scopus 로고    scopus 로고
    • Structural basis of pH-dependent antibody binding by the neonatal Fc receptor
    • Vaughn D. E., Bjorkman P. J. Structural basis of pH-dependent antibody binding by the neonatal Fc receptor. Structure. 6:1998;63-73.
    • (1998) Structure , vol.6 , pp. 63-73
    • Vaughn, D.E.1    Bjorkman, P.J.2
  • 38
    • 0030732164 scopus 로고    scopus 로고
    • Hereditary hemochromatosis: Effects of C282Y and H63D mutations on association with β2-microglobulin, intracellular processing, and cell surface expression of the HFE protein in COS-7 cells
    • Waheed A., Parkkila S., Zhou X. Y., Tomatsu S., Tsuchihashi Z., Feder J. N., Schatzman R. C., Britton R. S., Bacon B. R., Sly W. S. Hereditary hemochromatosis: effects of C282Y and H63D mutations on association with β2-microglobulin, intracellular processing, and cell surface expression of the HFE protein in COS-7 cells. Proc. Natl Acad. Sci. USA. 94:1997;12384-12389.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 12384-12389
    • Waheed, A.1    Parkkila, S.2    Zhou, X.Y.3    Tomatsu, S.4    Tsuchihashi, Z.5    Feder, J.N.6    Schatzman, R.C.7    Britton, R.S.8    Bacon, B.R.9    Sly, W.S.10
  • 39
    • 0029982521 scopus 로고    scopus 로고
    • Hematopoietic receptor complexes
    • Wells J. A., DeVos A. M. Hematopoietic receptor complexes. Annu. Rev. Biochem. 65:1996;609-634.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 609-634
    • Wells, J.A.1    Devos, A.M.2
  • 40
    • 0032006992 scopus 로고    scopus 로고
    • Unusual MHC-like molecules: CD1, Fc receptor, the hemochromatosis gene product, and viral homologs
    • Wilson I. A., Bjorkman P. J. Unusual MHC-like molecules: CD1, Fc receptor, the hemochromatosis gene product, and viral homologs. Curr. Opin. Immunol. 10:1998;67-73.
    • (1998) Curr. Opin. Immunol. , vol.10 , pp. 67-73
    • Wilson, I.A.1    Bjorkman, P.J.2


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