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Volumn 183, Issue 1, 1996, Pages 119-126

Evidence for a conformational change in a class II major histocompatibility complex molecule occuring in the same pH range where antigen binding is enhanced

Author keywords

[No Author keywords available]

Indexed keywords

MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2;

EID: 0030030896     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.183.1.119     Document Type: Article
Times cited : (52)

References (47)
  • 1
    • 0025813156 scopus 로고
    • The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation
    • Madden, D.R., J.C. Gorga, J.L. Strominger, and D.C. Wiley. 1991. The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation. Nature (Lond.). 353:321-325.
    • (1991) Nature (Lond.) , vol.353 , pp. 321-325
    • Madden, D.R.1    Gorga, J.C.2    Strominger, J.L.3    Wiley, D.C.4
  • 3
    • 0025300348 scopus 로고
    • The binary logic of antigen processing and presentation to T cells
    • Yewdell, J.W., and J R. Bennink. 1990. The binary logic of antigen processing and presentation to T cells. Cell. 62:203-206.
    • (1990) Cell , vol.62 , pp. 203-206
    • Yewdell, J.W.1    Bennink, J.R.2
  • 4
    • 0024324442 scopus 로고
    • Association of class I major histocompatibiliry heavy and light chains induced by viral peptides
    • Townsend, A., C. Oblen, J. Bastin, H.G. Ljunggren, L. Foster, and K. Karre. 1989. Association of class I major histocompatibiliry heavy and light chains induced by viral peptides. Nature (Lond.). 340:443-448.
    • (1989) Nature (Lond.) , vol.340 , pp. 443-448
    • Townsend, A.1    Oblen, C.2    Bastin, J.3    Ljunggren, H.G.4    Foster, L.5    Karre, K.6
  • 5
    • 0025609606 scopus 로고
    • The role of beta 2-microglobulin in peptide binding by class I molecules
    • Vinello, A., T.A. Potter, and L.A. Sherman. 1990. The role of beta 2-microglobulin in peptide binding by class I molecules. Science (Wash. DC). 250:1423-1426.
    • (1990) Science (Wash. DC) , vol.250 , pp. 1423-1426
    • Vinello, A.1    Potter, T.A.2    Sherman, L.A.3
  • 6
    • 0025835176 scopus 로고
    • Invariant chain targets HLA class II molecules to acidic endosomes containing internalized influenza virus
    • Lamb, C.A., J.W. Yewdell, J.R. Bennick, and P. Cresswell. 1991. Invariant chain targets HLA class II molecules to acidic endosomes containing internalized influenza virus. Proc. Natl. Acad. Sci. USA. 88:5998-6002.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5998-6002
    • Lamb, C.A.1    Yewdell, J.W.2    Bennick, J.R.3    Cresswell, P.4
  • 8
    • 0025331726 scopus 로고
    • Invariant chain association with HLA-DR molecules inhibits immunogenic peptide binding
    • Roche, P.A., and P. Cresswell. 1990. Invariant chain association with HLA-DR molecules inhibits immunogenic peptide binding. Nature (Lond.). 345:615-618.
    • (1990) Nature (Lond.) , vol.345 , pp. 615-618
    • Roche, P.A.1    Cresswell, P.2
  • 9
    • 0025313181 scopus 로고
    • Regulation of antigen presentation by acidic pH
    • Jensen, P.E. 1990. Regulation of antigen presentation by acidic pH. J. Exp. Med 171:1779-1784.
    • (1990) J. Exp. Med , vol.171 , pp. 1779-1784
    • Jensen, P.E.1
  • 10
    • 0025998830 scopus 로고
    • Enhanced binding of peptide antigen to purified class II major histocompatibility glycoproteins at acidic pH
    • Jensen, P.E. 1991. Enhanced binding of peptide antigen to purified class II major histocompatibility glycoproteins at acidic pH. J. Exp. Med. 174:1111-1120.
    • (1991) J. Exp. Med. , vol.174 , pp. 1111-1120
    • Jensen, P.E.1
  • 11
    • 0025898515 scopus 로고
    • Expression of a class II major histocompatibility complex (MHC) heterodimer in a lipid-linked form with enhanced peptide/soluble MHC complex formation at low pH
    • Wettstein, D.A., J.J. Boniface, P.A. Reay, H. Schild, and M M. Davis. 1991. Expression of a class II major histocompatibility complex (MHC) heterodimer in a lipid-linked form with enhanced peptide/soluble MHC complex formation at low pH. J. Exp. Med. 174:219-228.
    • (1991) J. Exp. Med. , vol.174 , pp. 219-228
    • Wettstein, D.A.1    Boniface, J.J.2    Reay, P.A.3    Schild, H.4    Davis, M.M.5
  • 12
    • 0026643116 scopus 로고
    • pH dependence and exchange of high and low responder peptides binding to a class II MHC molecule
    • Reay, P.A., D.A. Wettstein, and M.M. Davis. 1992. pH dependence and exchange of high and low responder peptides binding to a class II MHC molecule. EMBO (Eur. Mol. Biol. Organ.) J. 11:2829-2839.
    • (1992) EMBO (Eur. Mol. Biol. Organ.) J. , vol.11 , pp. 2829-2839
    • Reay, P.A.1    Wettstein, D.A.2    Davis, M.M.3
  • 13
    • 0026595058 scopus 로고
    • pH dependence of ehe interaction between immunogenic peptides and MHC class II molecules. Evidence for an acidic intracellular compartment being the organelle of interaction
    • Mouritsen, S., A.S. Hansen, B.L. Petersen, and S. Buus. 1992. pH dependence of ehe interaction between immunogenic peptides and MHC class II molecules. Evidence for an acidic intracellular compartment being the organelle of interaction. J. Immunol. 148:1438-1444.
    • (1992) J. Immunol. , vol.148 , pp. 1438-1444
    • Mouritsen, S.1    Hansen, A.S.2    Petersen, B.L.3    Buus, S.4
  • 15
    • 0025870669 scopus 로고
    • A role for peptide in determining MHC class II structure
    • Sadegh-Nasseri, S., and R.N. Germain. 1991. A role for peptide in determining MHC class II structure. Nature (Lond.). 353:167-170.
    • (1991) Nature (Lond.) , vol.353 , pp. 167-170
    • Sadegh-Nasseri, S.1    Germain, R.N.2
  • 16
    • 0026725145 scopus 로고
    • Conformational changes in mouse MHC class II proteins at acidic pH
    • Lee, J.M., C.M. Kay, and T.H. Watts. 1992. Conformational changes in mouse MHC class II proteins at acidic pH. Int. Immunol. 4:889-897.
    • (1992) Int. Immunol. , vol.4 , pp. 889-897
    • Lee, J.M.1    Kay, C.M.2    Watts, T.H.3
  • 17
    • 0025837691 scopus 로고
    • A first-order reaction controls the binding of antigenic peptides to major histocompatibility complex class II molecules
    • Witt, S.N., and H.M. McConnell. 1991. A first-order reaction controls the binding of antigenic peptides to major histocompatibility complex class II molecules. Proc. Natl. Acad. Sci. USA. 88:8164-8168.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8164-8168
    • Witt, S.N.1    McConnell, H.M.2
  • 19
    • 0008490055 scopus 로고
    • Mechanism of peptide release from major hisrocompatibility complex class II molecules
    • Witt, S.N., B.K. Clark, and H.M. McConnell. 1992. Mechanism of peptide release from major hisrocompatibility complex class II molecules. J. Am. Chem. Soc 114:9680-9682.
    • (1992) J. Am. Chem. Soc , vol.114 , pp. 9680-9682
    • Witt, S.N.1    Clark, B.K.2    McConnell, H.M.3
  • 20
    • 0025358699 scopus 로고
    • Refolding and reassembly of separate α and β chains of class II molecules of the major histocompatibility complex leads to increased peptide binding capactity
    • Dornmair, K., and H.M. McConnell. 1990. Refolding and reassembly of separate α and β chains of class II molecules of the major histocompatibility complex leads to increased peptide binding capactity. Proc Natl. Acad. Sci. USA. 87:4134-4138.
    • (1990) Proc Natl. Acad. Sci. USA , vol.87 , pp. 4134-4138
    • Dornmair, K.1    McConnell, H.M.2
  • 22
    • 0001369336 scopus 로고
    • A buffer solution for colorimetric comparison
    • McIlvaine, T.C. 1921. A buffer solution for colorimetric comparison. J. Biol. Chem. 49:183-187.
    • (1921) J. Biol. Chem. , vol.49 , pp. 183-187
    • McIlvaine, T.C.1
  • 24
    • 0027361113 scopus 로고
    • pH affects both the mechanism and specificity of peptide binding to a class II major histocompatibiliry molecule
    • Boniface, J.J., N.L. Allbritton, P.A. Reay, R.M. Kantor, L. Stryer, and M.M. Davis. 1993. pH affects both the mechanism and specificity of peptide binding to a class II major histocompatibiliry molecule. Biochemistry. 32:11761-11768.
    • (1993) Biochemistry , vol.32 , pp. 11761-11768
    • Boniface, J.J.1    Allbritton, N.L.2    Reay, P.A.3    Kantor, R.M.4    Stryer, L.5    Davis, M.M.6
  • 25
    • 0019800463 scopus 로고
    • Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity
    • Morrissey, J.H. 1981. Silver stain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity. Anal. Biochem. 117:307-310.
    • (1981) Anal. Biochem. , vol.117 , pp. 307-310
    • Morrissey, J.H.1
  • 26
    • 0026571278 scopus 로고
    • The human class II MHC protein HLA-DR1 assembles as empty αβ heterodimers in the absence of antigenic peptide
    • Stern, L.J., and D.C. Wiley. 1992. The human class II MHC protein HLA-DR1 assembles as empty αβ heterodimers in the absence of antigenic peptide. Cell. 68:465-477.
    • (1992) Cell , vol.68 , pp. 465-477
    • Stern, L.J.1    Wiley, D.C.2
  • 27
    • 0027291011 scopus 로고
    • Two-dimensional nuclear magnetic resonance analysis of a labeled peptide bound to a class II major histocompatibility complex molecule
    • Driscoll, P.C., J.D. Altman, J.J. Boniface, K. Sakaguchi, P.A. Reay, J.G. Omichinski, E. Appella, and M.M. Davis. 1993. Two-dimensional nuclear magnetic resonance analysis of a labeled peptide bound to a class II major histocompatibility complex molecule. J. Mol. Biol. 232.342-350.
    • (1993) J. Mol. Biol. , vol.232 , pp. 342-350
    • Driscoll, P.C.1    Altman, J.D.2    Boniface, J.J.3    Sakaguchi, K.4    Reay, P.A.5    Omichinski, J.G.6    Appella, E.7    Davis, M.M.8
  • 28
    • 0014354873 scopus 로고
    • Fluorescence spectroscopy of proteins
    • Stryer, L. 1968. Fluorescence spectroscopy of proteins. Science (Wash. DC) 162:526-533.
    • (1968) Science (Wash. DC) , vol.162 , pp. 526-533
    • Stryer, L.1
  • 29
    • 0014342841 scopus 로고
    • Quantitative estimation of protein binding site polarity. Fluorescence of N-arylaminonaphthalenesulfonates
    • Turner, D.C., and L. Brand. 1968. Quantitative estimation of protein binding site polarity. Fluorescence of N-arylaminonaphthalenesulfonates. Biochemistry. 7:3381-3390.
    • (1968) Biochemistry , vol.7 , pp. 3381-3390
    • Turner, D.C.1    Brand, L.2
  • 32
    • 0025938928 scopus 로고
    • Proposed molten globule intermediates in fd phage penetration and assembly
    • Dunker, A.K., L.D. Ensign, G.E. Arnold, and L.M. Roberts. 1991. Proposed molten globule intermediates in fd phage penetration and assembly. FEBS Lett. 292:275-278.
    • (1991) FEBS Lett. , vol.292 , pp. 275-278
    • Dunker, A.K.1    Ensign, L.D.2    Arnold, G.E.3    Roberts, L.M.4
  • 34
    • 0024595103 scopus 로고
    • Comparison of the secondary structure of human class I and class II major histocompatibility complex antigens by Fourier transform infrared and circular dichroism spectroscopy
    • Gorga, J.C., A. Dong, M.C. Manning, R.W. Woody, W.S. Caughey, and J.L. Strominger. 1989. Comparison of the secondary structure of human class I and class II major histocompatibility complex antigens by Fourier transform infrared and circular dichroism spectroscopy. Proc. Natl. Acad. Sci. USA. 86.2321-2325.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2321-2325
    • Gorga, J.C.1    Dong, A.2    Manning, M.C.3    Woody, R.W.4    Caughey, W.S.5    Strominger, J.L.6
  • 35
    • 0004155427 scopus 로고
    • W.H. Freeman & Co., New York
    • Stryer, L. 1988. Biochemistry, 3rd ed. W.H. Freeman & Co., New York. pp. 786-793.
    • (1988) Biochemistry, 3rd Ed. , pp. 786-793
    • Stryer, L.1
  • 36
    • 0025056497 scopus 로고
    • Defective processing and presentation of exogenous antigens in mutants with normal HLA class II genes
    • Mellins, E., L. Smith, B. Arp, T. Cotner, E. Celis, and D. Pious. 1990. Defective processing and presentation of exogenous antigens in mutants with normal HLA class II genes. Nature (Lond.). 343:71-74.
    • (1990) Nature (Lond.) , vol.343 , pp. 71-74
    • Mellins, E.1    Smith, L.2    Arp, B.3    Cotner, T.4    Celis, E.5    Pious, D.6
  • 38
    • 0028286474 scopus 로고
    • Protein conformational changes induced by 1,1′-bis(4-anilino-5-naphthalenesulfonic acid): Preferential binding to the molten globule of DnaK
    • Shi, L., D.R. Palleros, and A.L. Fink. 1994. Protein conformational changes induced by 1,1′-bis(4-anilino-5-naphthalenesulfonic acid): preferential binding to the molten globule of DnaK. Biochemistry. 33:7536-7546.
    • (1994) Biochemistry , vol.33 , pp. 7536-7546
    • Shi, L.1    Palleros, D.R.2    Fink, A.L.3
  • 39
    • 0028466243 scopus 로고
    • Solid evidence for molten globules
    • Dobson, C.M. 1994. Solid evidence for molten globules. Curr. Biol. 4:636-640.
    • (1994) Curr. Biol. , vol.4 , pp. 636-640
    • Dobson, C.M.1
  • 41
    • 0026742999 scopus 로고
    • HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells
    • Schaiff, W.T., K.A. Hruska, Jr., D.W. McCourt, M. Green, and B.D. Schwartz. 1992. HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells. J. Exp. Med. 176:657-666.
    • (1992) J. Exp. Med. , vol.176 , pp. 657-666
    • Schaiff, W.T.1    Hruska Jr., K.A.2    McCourt, D.W.3    Green, M.4    Schwartz, B.D.5
  • 42
    • 0028334547 scopus 로고
    • Conformanonal specificity of the chaperonin GroEL for the compact folding intermediates of α-lactalbumin
    • Hayer-Hartl, M.K., J.J. Ewbink, T.E. Creighton, and F.U. Haiti. 1994. Conformanonal specificity of the chaperonin GroEL for the compact folding intermediates of α-lactalbumin. EMBO (Eur. Mol. Biol. Organ.) J. 13:3192-3202.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 3192-3202
    • Hayer-Hartl, M.K.1    Ewbink, J.J.2    Creighton, T.E.3    Haiti, F.U.4
  • 43
    • 0026416043 scopus 로고
    • Chaperonin-mediated protein folding at the surface of groEL through a "molten globule"-like intermediate
    • Martin, J., T. Langer, R. Boteva, A. Schramel, A.L. Horwich, and F.U. Hard. 1991. Chaperonin-mediated protein folding at the surface of groEL through a "molten globule"-like intermediate. Nature (Lond.). 352:36-42.
    • (1991) Nature (Lond.) , vol.352 , pp. 36-42
    • Martin, J.1    Langer, T.2    Boteva, R.3    Schramel, A.4    Horwich, A.L.5    Hard, F.U.6
  • 45
    • 0026088067 scopus 로고
    • 2-microglobulin is necessary for Db class I major histocompanbility complex binding of an exogenous influenza peptide
    • 2-microglobulin is necessary for Db class I major histocompanbility complex binding of an exogenous influenza peptide. Proc. Natl Acad. Sci. USA. 88:301-304.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 301-304
    • Rock, K.L.1    Gamble, S.R.2    Rothstein, L.E.3    Benacerraf, B.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.