메뉴 건너뛰기




Volumn 338, Issue 5, 2004, Pages 921-941

Solution structure determination of monomeric human IgA2 by X-ray and neutron scattering, analytical ultracentrifugation and constrained modelling: A comparison with monomeric human IgA1

Author keywords

Analytical ultracentrifugation; Antibody structure; Fc RI, receptor for Fc fragment of IgA; IgA, immunoglobulin A; IgG, immunoglobulin G; Immunoglobulin A; Neutron scattering; X ray scattering

Indexed keywords

IMMUNOGLOBULIN A1; IMMUNOGLOBULIN A2; IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN FC FRAGMENT; MONOMER; RECOMBINANT PROTEIN;

EID: 2142643646     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.03.007     Document Type: Article
Times cited : (98)

References (68)
  • 1
    • 0025007135 scopus 로고
    • The structure and function of human IgA
    • Kerr M.A. The structure and function of human IgA. Biochem. J. 271:1990;285-296.
    • (1990) Biochem. J. , vol.271 , pp. 285-296
    • Kerr, M.A.1
  • 3
    • 0022566877 scopus 로고
    • Immunoglobulin A: Strategic defense initiative at the mucosal surface
    • Underdown B.J., Schiff J.M. Immunoglobulin A: strategic defense initiative at the mucosal surface. Annu. Rev. Immunol. 4:1986;389-417.
    • (1986) Annu. Rev. Immunol. , vol.4 , pp. 389-417
    • Underdown, B.J.1    Schiff, J.M.2
  • 6
    • 0000265215 scopus 로고    scopus 로고
    • Fcα receptors
    • P.L. Ogra, J. Mestecky, M.E. Lamm, W. Strober, J.R. McGhee, & J. Bienenstock. San Diego: Academic Press Inc.
    • Kerr M.A., Woof J.M. Fcα receptors. Ogra P.L., Mestecky J., Lamm M.E., Strober W., McGhee J.R., Bienenstock J. Mucosal Immunology. 2nd edit. 1999;213-224 Academic Press Inc. San Diego.
    • (1999) Mucosal Immunology 2nd Edit. , pp. 213-224
    • Kerr, M.A.1    Woof, J.M.2
  • 8
    • 0001743458 scopus 로고    scopus 로고
    • Biological activities of IgA
    • P.L. Ogra, J. Mestecky, M.E. Lamm, W. Strober, J.R. McGhee, & J. Bienenstock. San Diego: Academic Press Inc.
    • Russell M.W., Kilian M., Lamm M.E. Biological activities of IgA. Ogra P.L., Mestecky J., Lamm M.E., Strober W., McGhee J.R., Bienenstock J. Mucosal Immunology. 2nd edit. 1999;225-240 Academic Press Inc. San Diego.
    • (1999) Mucosal Immunology 2nd Edit. , pp. 225-240
    • Russell, M.W.1    Kilian, M.2    Lamm, M.E.3
  • 9
    • 0035986876 scopus 로고    scopus 로고
    • Adaptive evolution of the IgA hinge region in primates
    • Sumiyama K., Saitou N., Ueda S. Adaptive evolution of the IgA hinge region in primates. Mol. Biol. Evol. 19:2002;1093-1099.
    • (2002) Mol. Biol. Evol. , vol.19 , pp. 1093-1099
    • Sumiyama, K.1    Saitou, N.2    Ueda, S.3
  • 10
    • 0033548612 scopus 로고    scopus 로고
    • The Fab and Fc fragments of IgA1 exhibit a different arrangement from that in IgG: A study by X-ray and neutron solution scattering and homology modelling
    • Boehm M.K., Woof J.M., Kerr M.A., Perkins S.J. The Fab and Fc fragments of IgA1 exhibit a different arrangement from that in IgG: a study by X-ray and neutron solution scattering and homology modelling. J. Mol. Biol. 286:1999;1421-1447.
    • (1999) J. Mol. Biol. , vol.286 , pp. 1421-1447
    • Boehm, M.K.1    Woof, J.M.2    Kerr, M.A.3    Perkins, S.J.4
  • 11
    • 0028179891 scopus 로고
    • Divergence of human α-chain constant region gene sequences. A novel recombinant α2 gene
    • Chintalacharuvu K.R., Raines M., Morrison S.L. Divergence of human α-chain constant region gene sequences. A novel recombinant α2 gene. J. Immunol. 152:1994;5299-5304.
    • (1994) J. Immunol. , vol.152 , pp. 5299-5304
    • Chintalacharuvu, K.R.1    Raines, M.2    Morrison, S.L.3
  • 12
    • 0028114209 scopus 로고
    • Carbohydrate heterogeneity of human myeloma proteins of the IgA1 and IgA2 subclasses
    • Endo T., Mestecky J., Kulhavy R., Kobata A. Carbohydrate heterogeneity of human myeloma proteins of the IgA1 and IgA2 subclasses. Mol. Immunol. 31:1994;1415-1422.
    • (1994) Mol. Immunol. , vol.31 , pp. 1415-1422
    • Endo, T.1    Mestecky, J.2    Kulhavy, R.3    Kobata, A.4
  • 13
    • 0031915973 scopus 로고    scopus 로고
    • The glycosylation and structure of human serum IgA1, Fab and Fc regions and the role of N-glycosylation on Fcα receptor interactions
    • Mattu T.J., Pleass R.J., Willis A.C., Kilian M., Wormald M.R., Lellouch A.C., et al. The glycosylation and structure of human serum IgA1, Fab and Fc regions and the role of N-glycosylation on Fcα receptor interactions. J. Biol. Chem. 273:1998;2260-2272.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2260-2272
    • Mattu, T.J.1    Pleass, R.J.2    Willis, A.C.3    Kilian, M.4    Wormald, M.R.5    Lellouch, A.C.6
  • 15
    • 0030014069 scopus 로고    scopus 로고
    • Biological significance of IgA1 proteases in bacterial colonization and pathogenesis: Critical evaluation of experimental evidence
    • Kilian M., Reinholdt J., Lomholt H., Poulsen K., Frandsen E.V.G. Biological significance of IgA1 proteases in bacterial colonization and pathogenesis: critical evaluation of experimental evidence. APMIS. 104:1996;321-338.
    • (1996) APMIS , vol.104 , pp. 321-338
    • Kilian, M.1    Reinholdt, J.2    Lomholt, H.3    Poulsen, K.4    Frandsen, E.V.G.5
  • 16
    • 0028129261 scopus 로고
    • A human T-cell receptor recognises O-linked sugars from the hinge region of human IgA1 and IgD
    • Rudd P.M., Fortune F., Patel T., Parekh R.B., Dwek R.A., Lehner T. A human T-cell receptor recognises O-linked sugars from the hinge region of human IgA1 and IgD. Immunology. 83:1994;99-106.
    • (1994) Immunology , vol.83 , pp. 99-106
    • Rudd, P.M.1    Fortune, F.2    Patel, T.3    Parekh, R.B.4    Dwek, R.A.5    Lehner, T.6
  • 18
    • 0037103328 scopus 로고    scopus 로고
    • Selective adherence of IgA to murine Peyer's patch M cells: Evidence for a novel IgA receptor
    • Mantis N.J., Cheung M.C., Chintalacharuvu K.R., Rey J., Corthesy B., Neutra M.R. Selective adherence of IgA to murine Peyer's patch M cells: evidence for a novel IgA receptor. J. Immunol. 169:2002;1844-1851.
    • (2002) J. Immunol. , vol.169 , pp. 1844-1851
    • Mantis, N.J.1    Cheung, M.C.2    Chintalacharuvu, K.R.3    Rey, J.4    Corthesy, B.5    Neutra, M.R.6
  • 20
    • 0037497304 scopus 로고    scopus 로고
    • Insights into IgA-mediated immune responses from the crystal structures of human FcαRI and its complex with IgA1-Fc
    • Herr A.B., Ballister E.R., Bjorkman P.J. Insights into IgA-mediated immune responses from the crystal structures of human FcαRI and its complex with IgA1-Fc. Nature. 423:2003;614-620.
    • (2003) Nature , vol.423 , pp. 614-620
    • Herr, A.B.1    Ballister, E.R.2    Bjorkman, P.J.3
  • 22
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein a from Staphylococcus aureus at 2.9 and 2.8 Å resolution
    • Deisenhofer J. Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9 and 2.8 Å resolution. Biochemistry. 20:1981;2361-2370.
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 25
    • 0033501383 scopus 로고    scopus 로고
    • Comparison of intact antibody structures and the implications for effector function
    • Harris L.J., Larson S.B., McPherson A. Comparison of intact antibody structures and the implications for effector function. Advan. Immunol. 72:1999;191-208.
    • (1999) Advan. Immunol. , vol.72 , pp. 191-208
    • Harris, L.J.1    Larson, S.B.2    McPherson, A.3
  • 26
    • 0015247268 scopus 로고
    • The three-dimensional conformation of γm and γa globulin molecules
    • Feinstein A., Munn E.A., Richardson N.E. The three-dimensional conformation of γM and γA globulin molecules. Ann. N. Y. Acad. Sci. 190:1971;104-121.
    • (1971) Ann. N. Y. Acad. Sci. , vol.190 , pp. 104-121
    • Feinstein, A.1    Munn, E.A.2    Richardson, N.E.3
  • 27
    • 0032532015 scopus 로고    scopus 로고
    • Comparisons of the ability of human IgG3 hinge mutants, IgM, IgE and IgA2, to form small immune complexes: A role for flexibility and geometry
    • Roux K.H., Strelets L., Brekke O.H., Sandlie I., Michaelsen T.E. Comparisons of the ability of human IgG3 hinge mutants, IgM, IgE and IgA2, to form small immune complexes: a role for flexibility and geometry. J. Immunol. 161:1998;4083-4090.
    • (1998) J. Immunol. , vol.161 , pp. 4083-4090
    • Roux, K.H.1    Strelets, L.2    Brekke, O.H.3    Sandlie, I.4    Michaelsen, T.E.5
  • 28
    • 0029131402 scopus 로고
    • Demonstration by pulsed neutron scattering that the arrangement of the Fab and Fc fragments in the overall structures of bovine IgG1 and IgG2 in solution is similar
    • Mayans M.O., Coadwell W.J., Beale D., Symons D., Perkins S.J. Demonstration by pulsed neutron scattering that the arrangement of the Fab and Fc fragments in the overall structures of bovine IgG1 and IgG2 in solution is similar. Biochem. J. 311:1995;283-291.
    • (1995) Biochem. J. , vol.311 , pp. 283-291
    • Mayans, M.O.1    Coadwell, W.J.2    Beale, D.3    Symons, D.4    Perkins, S.J.5
  • 29
    • 0037954130 scopus 로고    scopus 로고
    • The extended multidomain solution structures of the complement protein Crry and its chimeric conjugate Crry-Ig by scattering, analytical ultracentrifugation and constrained modelling: Implications for function and therapy
    • Aslam M., Guthridge J.M., Hack B.K., Quigg R.J., Holers V.M., Perkins S.J. The extended multidomain solution structures of the complement protein Crry and its chimeric conjugate Crry-Ig by scattering, analytical ultracentrifugation and constrained modelling: implications for function and therapy. J. Mol. Biol. 329:2003;525-550.
    • (2003) J. Mol. Biol. , vol.329 , pp. 525-550
    • Aslam, M.1    Guthridge, J.M.2    Hack, B.K.3    Quigg, R.J.4    Holers, V.M.5    Perkins, S.J.6
  • 31
    • 0027485053 scopus 로고
    • Purification and characterization of chimeric human IgA1 and IgA2 expressed in COS and Chinese hamster ovary cells
    • Morton H.C., Atkin J.D., Owens R.J., Woof J.M. Purification and characterization of chimeric human IgA1 and IgA2 expressed in COS and Chinese hamster ovary cells. J. Immunol. 151:1993;4743-4752.
    • (1993) J. Immunol. , vol.151 , pp. 4743-4752
    • Morton, H.C.1    Atkin, J.D.2    Owens, R.J.3    Woof, J.M.4
  • 32
    • 0028828789 scopus 로고
    • Bent domain structure of recombinant human IgE-Fc in solution by X-ray and neutron scattering in conjunction with an automated curve fitting procedure
    • Beavil A.J., Young R.J., Sutton B.J., Perkins S.J. Bent domain structure of recombinant human IgE-Fc in solution by X-ray and neutron scattering in conjunction with an automated curve fitting procedure. Biochemistry. 34:1995;14449-14461.
    • (1995) Biochemistry , vol.34 , pp. 14449-14461
    • Beavil, A.J.1    Young, R.J.2    Sutton, B.J.3    Perkins, S.J.4
  • 33
    • 0023049766 scopus 로고
    • Protein volumes and hydration effects: The calculation of partial specific volumes, neutron scattering matchpoints and 280 nm absorption coefficients for proteins and glycoproteins from amino acid sequences
    • Perkins S.J. Protein volumes and hydration effects: the calculation of partial specific volumes, neutron scattering matchpoints and 280 nm absorption coefficients for proteins and glycoproteins from amino acid sequences. Eur. J. Biochem. 157:1986;169-180.
    • (1986) Eur. J. Biochem. , vol.157 , pp. 169-180
    • Perkins, S.J.1
  • 34
    • 0035965873 scopus 로고    scopus 로고
    • X-ray and neutron scattering analyses of hydration shells: A molecular interpretation based on sequence predictions and modelling fits
    • Perkins S.J. X-ray and neutron scattering analyses of hydration shells: a molecular interpretation based on sequence predictions and modelling fits. Biophys. Chem. 93:2001;129-139.
    • (2001) Biophys. Chem. , vol.93 , pp. 129-139
    • Perkins, S.J.1
  • 35
    • 0016196035 scopus 로고
    • Gross conformation of human secretory immunoglobulin a and its component parts
    • Björk I., Lindh E. Gross conformation of human secretory immunoglobulin A and its component parts. Eur. J. Biochem. 45:1974;135-145.
    • (1974) Eur. J. Biochem. , vol.45 , pp. 135-145
    • Björk, I.1    Lindh, E.2
  • 36
    • 0030587893 scopus 로고    scopus 로고
    • Residues critical for H-L disulphide bond formation in human IgA1 and IgA2
    • Chintalacharuvu K.R., Morrison S.L. Residues critical for H-L disulphide bond formation in human IgA1 and IgA2. J. Immunol. 157:1996;3443-3449.
    • (1996) J. Immunol. , vol.157 , pp. 3443-3449
    • Chintalacharuvu, K.R.1    Morrison, S.L.2
  • 38
    • 0037470618 scopus 로고    scopus 로고
    • Bivalent binding of IgA1 to FcαRI suggests a mechanism for cytokine activation of IgA phagocytosis
    • Herr A.B., White C.L., Milburn C., Wu C., Bjorkman P.J. Bivalent binding of IgA1 to FcαRI suggests a mechanism for cytokine activation of IgA phagocytosis. J. Mol. Biol. 327:2003;645-657.
    • (2003) J. Mol. Biol. , vol.327 , pp. 645-657
    • Herr, A.B.1    White, C.L.2    Milburn, C.3    Wu, C.4    Bjorkman, P.J.5
  • 39
    • 0038443992 scopus 로고    scopus 로고
    • Structural and functional consequences of cleavage of human secretory and human serum immunoglobulin A1 by proteinases from Proteus mirabilis and Neisseria meningitides
    • Almogren A., Senior B.W., Loomes L.M., Kerr M.A. Structural and functional consequences of cleavage of human secretory and human serum immunoglobulin A1 by proteinases from Proteus mirabilis and Neisseria meningitides. Infect. Immun. 71:2003;3349-3356.
    • (2003) Infect. Immun. , vol.71 , pp. 3349-3356
    • Almogren, A.1    Senior, B.W.2    Loomes, L.M.3    Kerr, M.A.4
  • 40
    • 0037369766 scopus 로고    scopus 로고
    • Amino acid sequence requirements in the hinge of human immunoglobulin A1 (IgA1) for cleavage by streptococcal IgA1 proteases
    • Batten M.R., Senior B.W., Kilian M., Woof J.M. Amino acid sequence requirements in the hinge of human immunoglobulin A1 (IgA1) for cleavage by streptococcal IgA1 proteases. Infect. Immun. 71:2003;1462-1469.
    • (2003) Infect. Immun. , vol.71 , pp. 1462-1469
    • Batten, M.R.1    Senior, B.W.2    Kilian, M.3    Woof, J.M.4
  • 42
    • 0027154092 scopus 로고
    • Three-dimensional structure of a human immunoglobulin with a hinge deletion
    • Guddat L.W., Herron J.N., Edmundson A.B. Three-dimensional structure of a human immunoglobulin with a hinge deletion. Proc. Natl Acad. Sci. USA. 90:1993;4271-4275.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 4271-4275
    • Guddat, L.W.1    Herron, J.N.2    Edmundson, A.B.3
  • 44
    • 0029924133 scopus 로고    scopus 로고
    • Localisation of the binding site for the monocyte immunoglobulin (Ig) A-Fc receptor (CD89) to the domain boundary between Cα2 and Cα3 in human IgA1
    • Carayannopoulos L., Hexham J.M., Capra J.D. Localisation of the binding site for the monocyte immunoglobulin (Ig) A-Fc receptor (CD89) to the domain boundary between Cα2 and Cα3 in human IgA1. J. Expt. Med. 183:1996;1579-1586.
    • (1996) J. Expt. Med. , vol.183 , pp. 1579-1586
    • Carayannopoulos, L.1    Hexham, J.M.2    Capra, J.D.3
  • 45
    • 0033551694 scopus 로고    scopus 로고
    • H3 domain interface of IgA essential for interaction with the human Fcα receptor (FcαRI) CD89
    • H3 domain interface of IgA essential for interaction with the human Fcα receptor (FcαRI) CD89. J. Biol. Chem. 274:1999;23508-23514.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23508-23514
    • Pleass, R.J.1    Dunlop, J.I.2    Anderson, C.M.3    Woof, J.M.4
  • 46
    • 0020591320 scopus 로고
    • Allotypic and isotypic aspects of immunoglobulin a
    • van Loghem E., Biewenga J. Allotypic and isotypic aspects of immunoglobulin A. Mol. Immunol. 20:1983;1001-1007.
    • (1983) Mol. Immunol. , vol.20 , pp. 1001-1007
    • Van Loghem, E.1    Biewenga, J.2
  • 47
    • 0016023069 scopus 로고
    • Special characteristics of the IgA2 subclass
    • J. Mestecky, & A.R. Lawton. New York: Plenum Press
    • Jerry L.M., Kunkel H.G. Special characteristics of the IgA2 subclass. Mestecky J., Lawton A.R. The Immunoglobulin A System. 1974;151-160 Plenum Press, New York.
    • (1974) The Immunoglobulin a System , pp. 151-160
    • Jerry, L.M.1    Kunkel, H.G.2
  • 48
    • 0026560477 scopus 로고
    • Effects of limited reduction on disulphide bonds in human IgA1 and IgA1 fragments
    • Biewenga J., van Run P.E.M. Effects of limited reduction on disulphide bonds in human IgA1 and IgA1 fragments. Mol. Immunol. 29:1992;327-334.
    • (1992) Mol. Immunol. , vol.29 , pp. 327-334
    • Biewenga, J.1    Van Run, P.E.M.2
  • 49
    • 0025923189 scopus 로고
    • Purification and characterisation of human immunoglobulin IgA1 and IgA2 isotypes from serum
    • Loomes L.M., Stewart W.W., Mazengera R.L., Senior B.W., Kerr M.A. Purification and characterisation of human immunoglobulin IgA1 and IgA2 isotypes from serum. J. Immunol. Methods. 141:1991;209-218.
    • (1991) J. Immunol. Methods , vol.141 , pp. 209-218
    • Loomes, L.M.1    Stewart, W.W.2    Mazengera, R.L.3    Senior, B.W.4    Kerr, M.A.5
  • 50
    • 0013642465 scopus 로고    scopus 로고
    • Purification and characterization of human serum and secretory IgA1 and IgA2 using jacalin
    • Kerr M.A., Loomes L.M., Bonner B.C., Hutchings A.B., Senior B.W. Purification and characterization of human serum and secretory IgA1 and IgA2 using jacalin. Methods Mol. Med. 9:1997;265-278.
    • (1997) Methods Mol. Med. , vol.9 , pp. 265-278
    • Kerr, M.A.1    Loomes, L.M.2    Bonner, B.C.3    Hutchings, A.B.4    Senior, B.W.5
  • 53
    • 0011943275 scopus 로고
    • Development of the small-angle diffractometer LOQ at the ISIS pulsed neutron source
    • Dubna, 1st-4th September 1992. Report E3-93-65, Joint Institute for Nuclear Research, Dubna.
    • Heenan, R. K. & King, S. M. (1993). Development of the small-angle diffractometer LOQ at the ISIS pulsed neutron source. In Proceedings of an International Seminar on Structural Investigations at Pulsed Neutron Sources, Dubna, 1st-4th September 1992. Report E3-93-65, Joint Institute for Nuclear Research, Dubna.
    • (1993) Proceedings of An International Seminar on Structural Investigations at Pulsed Neutron Sources
    • Heenan, R.K.1    King, S.M.2
  • 54
    • 0003702492 scopus 로고
    • O. Glatter, & O. Kratky. New York: Academic Press
    • Glatter O., Kratky O. Small-angle X-ray Scattering. 1982;Academic Press, New York.
    • (1982) Small-angle X-ray Scattering
  • 55
    • 0015891931 scopus 로고
    • Shape and volume of anti-poly(D-alanyl) antibodies in the presence and absence of tetra-D-alanine as followed by small-angle X-ray scattering
    • Pilz I., Kratky O., Licht A., Sela M. Shape and volume of anti-poly(D-alanyl) antibodies in the presence and absence of tetra-D-alanine as followed by small-angle X-ray scattering. Biochemistry. 12:1973;4998-5005.
    • (1973) Biochemistry , vol.12 , pp. 4998-5005
    • Pilz, I.1    Kratky, O.2    Licht, A.3    Sela, M.4
  • 56
    • 0026244044 scopus 로고
    • GNOM-a program package for small-angle scattering data-processing
    • Semenyuk A.V., Svergun D.I. GNOM-a program package for small-angle scattering data-processing. J. Appl. Crystallog. 24:1991;537-540.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 537-540
    • Semenyuk, A.V.1    Svergun, D.I.2
  • 57
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • S.E. Harding, A.J. Rowe, & J.C. Horton. Cambridge, UK: The Royal Society of Chemistry
    • Laue T.M., Shah B.D., Ridgeway T.M., Pelletier S.L. Computer-aided interpretation of analytical sedimentation data for proteins. Harding S.E., Rowe A.J., Horton J.C. Analytical Ultracentrifugation in Biochemistry and Polymer Science. 1992;90-125 The Royal Society of Chemistry, Cambridge, UK.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 58
    • 0034654352 scopus 로고    scopus 로고
    • A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions
    • Philo J. A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions. Anal. Biochem. 279:2000;151-163.
    • (2000) Anal. Biochem. , vol.279 , pp. 151-163
    • Philo, J.1
  • 59
    • 0031688168 scopus 로고    scopus 로고
    • Sedimentation analysis of non-interacting and self-associating solutes using numerical solutions to the Lamm equation
    • Schuck P. Sedimentation analysis of non-interacting and self-associating solutes using numerical solutions to the Lamm equation. Biophys. J. 75:1998;1503-1512.
    • (1998) Biophys. J. , vol.75 , pp. 1503-1512
    • Schuck, P.1
  • 60
    • 0028835227 scopus 로고
    • Three-dimensional structures of the Fab fragment of murine N1G9 antibody from the primary immune response and of its complex with (4-hydroxy-3- nitrophenyl)acetate
    • Mizutani R., Miura K., Nakayama T., Shimada I., Arata Y., Satow Y. Three-dimensional structures of the Fab fragment of murine N1G9 antibody from the primary immune response and of its complex with (4-hydroxy-3-nitrophenyl) acetate. J. Mol. Biol. 254:1995;208-222.
    • (1995) J. Mol. Biol. , vol.254 , pp. 208-222
    • Mizutani, R.1    Miura, K.2    Nakayama, T.3    Shimada, I.4    Arata, Y.5    Satow, Y.6
  • 61
    • 15844387253 scopus 로고    scopus 로고
    • Structural studies of human autoantibodies-crystal-structure of a thyroid peroxidase autoantibody Fab
    • Chacko S., Padlan E.A., Portolano S., McLachlan S.M., Rapoport B. Structural studies of human autoantibodies-crystal-structure of a thyroid peroxidase autoantibody Fab. J. Biol. Chem. 271:1996;12191-12198.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12191-12198
    • Chacko, S.1    Padlan, E.A.2    Portolano, S.3    McLachlan, S.M.4    Rapoport, B.5
  • 62
  • 64
    • 0031587295 scopus 로고    scopus 로고
    • Pentameric and decameric structures in solution of the serum amyloid P component by X-ray and neutron scattering and molecular modelling analyses
    • Ashton A.W., Boehm M.K., Gallimore J.R., Pepys M.B., Perkins S.J. Pentameric and decameric structures in solution of the serum amyloid P component by X-ray and neutron scattering and molecular modelling analyses. J. Mol. Biol. 272:1997;408-422.
    • (1997) J. Mol. Biol. , vol.272 , pp. 408-422
    • Ashton, A.W.1    Boehm, M.K.2    Gallimore, J.R.3    Pepys, M.B.4    Perkins, S.J.5
  • 65
    • 0021112502 scopus 로고
    • Low resolution structural studies of mitochondrial ubiquinol-cytochrome c reductase in detergent solutions by neutron scattering
    • Perkins S.J., Weiss H. Low resolution structural studies of mitochondrial ubiquinol-cytochrome c reductase in detergent solutions by neutron scattering. J. Mol. Biol. 168:1983;847-866.
    • (1983) J. Mol. Biol. , vol.168 , pp. 847-866
    • Perkins, S.J.1    Weiss, H.2
  • 66
    • 0017403408 scopus 로고
    • Hydrodynamic properties of macromolecular complexes. I. Translation
    • Garcia de la Torre J., Bloomfield V.A. Hydrodynamic properties of macromolecular complexes. I. Translation. Biopolymers. 16:1977;1747-1761.
    • (1977) Biopolymers , vol.16 , pp. 1747-1761
    • Garcia De La Torre, J.1    Bloomfield, V.A.2
  • 67
    • 0017750547 scopus 로고
    • Hydrodynamics of macromolecular complexes. III. Bacterial viruses
    • Garcia de la Torre J., Bloomfield V.A. Hydrodynamics of macromolecular complexes. III. Bacterial viruses. Biopolymers. 16:1977;1779-1793.
    • (1977) Biopolymers , vol.16 , pp. 1779-1793
    • Garcia De La Torre, J.1    Bloomfield, V.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.