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Volumn 391, Issue 1, 2010, Pages 947-951

Global structure of HIV-1 neutralizing antibody IgG1 b12 is asymmetric

Author keywords

Guinier approximation; HIV 1 neutralizing antibody; Kratky analysis; Molecular modeling; Small angle X ray scattering

Indexed keywords

HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; IMMUNOGLOBULIN G1 B12 ANTIBODY; NEUTRALIZING ANTIBODY; UNCLASSIFIED DRUG;

EID: 72949106692     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.11.170     Document Type: Article
Times cited : (20)

References (24)
  • 3
    • 0034864776 scopus 로고    scopus 로고
    • Antibody protects macaques against vaginal challenge with a pathogenic R5 simian/human immunodeficiency virus at serum levels giving complete neutralization in vitro
    • Parren P.W., Marx P.A., Hessell A.J., Luckay A., Harouse J., Cheng-Mayer C., Moore J.P., and Burton D.R. Antibody protects macaques against vaginal challenge with a pathogenic R5 simian/human immunodeficiency virus at serum levels giving complete neutralization in vitro. J. Virol. 75 (2001) 8340-8347
    • (2001) J. Virol. , vol.75 , pp. 8340-8347
    • Parren, P.W.1    Marx, P.A.2    Hessell, A.J.3    Luckay, A.4    Harouse, J.5    Cheng-Mayer, C.6    Moore, J.P.7    Burton, D.R.8
  • 4
    • 13844255333 scopus 로고    scopus 로고
    • Broadly neutralizing anti-HIV antibody 4E10 recognizes a helical conformation of a highly conserved fusion-associated motif in gp41
    • Cardoso R.M., Zwick M.B., Stanfield R.L., Kunert R., Binley J.M., Katinger H., Burton D.R., and Wilson I.A. Broadly neutralizing anti-HIV antibody 4E10 recognizes a helical conformation of a highly conserved fusion-associated motif in gp41. Immunity 22 (2005) 163-173
    • (2005) Immunity , vol.22 , pp. 163-173
    • Cardoso, R.M.1    Zwick, M.B.2    Stanfield, R.L.3    Kunert, R.4    Binley, J.M.5    Katinger, H.6    Burton, D.R.7    Wilson, I.A.8
  • 8
    • 0035176595 scopus 로고    scopus 로고
    • Crystallization and preliminary structure determination of an intact human immunoglobulin, b12: an antibody that broadly neutralizes primary isolates of HIV-1
    • Saphire E.O., Parren P.W., Barbas III C.F., Burton D.R., and Wilson I.A. Crystallization and preliminary structure determination of an intact human immunoglobulin, b12: an antibody that broadly neutralizes primary isolates of HIV-1. Acta Crystallogr. D Biol. Crystallogr. 57 (2001) 168-171
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 168-171
    • Saphire, E.O.1    Parren, P.W.2    Barbas III, C.F.3    Burton, D.R.4    Wilson, I.A.5
  • 10
    • 0025838698 scopus 로고
    • A large array of human monoclonal antibodies to type 1 human immunodeficiency virus from combinatorial libraries of asymptomatic seropositive individuals
    • Burton D.R., Barbas III C.F., Persson M.A., Koenig S., Chanock R.M., and Lerner R.A. A large array of human monoclonal antibodies to type 1 human immunodeficiency virus from combinatorial libraries of asymptomatic seropositive individuals. Proc. Natl. Acad. Sci. USA 88 (1991) 10134-10137
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10134-10137
    • Burton, D.R.1    Barbas III, C.F.2    Persson, M.A.3    Koenig, S.4    Chanock, R.M.5    Lerner, R.A.6
  • 14
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun D.I. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 25 (1992) 495-503
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 15
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun D.I. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76 (1999) 2879-2886
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 16
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov V.V., and Svergun D.I. Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Crystallogr. 25 (2003) 860-864
    • (2003) J. Appl. Crystallogr. , vol.25 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 17
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • Kozin M.B., and Svergun D.I. Automated matching of high- and low-resolution structural models. J. Appl. Crystallogr. 34 (2001) 33-41
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 18
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D., Barberato C., and Koch M.H.J. CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 28 (1995) 768-773
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 19
    • 0029876864 scopus 로고    scopus 로고
    • Conformational characterization of DnaK and its complexes by small-angle X-ray scattering
    • Shi L., Kataoka M., and Fink A.L. Conformational characterization of DnaK and its complexes by small-angle X-ray scattering. Biochemistry 35 (1996) 3297-3308
    • (1996) Biochemistry , vol.35 , pp. 3297-3308
    • Shi, L.1    Kataoka, M.2    Fink, A.L.3
  • 20
    • 0037120759 scopus 로고    scopus 로고
    • Lysozyme viscoelastic matrices in tetramethylurea/water media: a small angle X-ray scattering study
    • da Silva M.A., Itri R., and Areas E.P. Lysozyme viscoelastic matrices in tetramethylurea/water media: a small angle X-ray scattering study. Biophys. Chem. 99 (2002) 169-179
    • (2002) Biophys. Chem. , vol.99 , pp. 169-179
    • da Silva, M.A.1    Itri, R.2    Areas, E.P.3
  • 21
    • 35648995341 scopus 로고    scopus 로고
    • Conformational analysis of the leukocyte-specific EF-hand protein p65/L-plastin by X-ray scattering in solution
    • Shinomiya H., Shinjo M., Fengzhi L., Asano Y., and Kihara H. Conformational analysis of the leukocyte-specific EF-hand protein p65/L-plastin by X-ray scattering in solution. Biophys. Chem. 131 (2007) 36-42
    • (2007) Biophys. Chem. , vol.131 , pp. 36-42
    • Shinomiya, H.1    Shinjo, M.2    Fengzhi, L.3    Asano, Y.4    Kihara, H.5
  • 22
    • 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.B., and 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 Pt. 1 (1995) 283-291
    • (1995) Biochem. J. , vol.311 , Issue.PART 1 , pp. 283-291
    • Mayans, M.O.1    Coadwell, W.J.2    Beale, D.3    Symons, D.B.4    Perkins, S.J.5
  • 23
    • 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., and 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
  • 24
    • 2142643646 scopus 로고    scopus 로고
    • Solution structure determination of monomeric human IgA2 by X-ray and neutron scattering, analytical ultracentrifugation and constrained modelling: a comparison with monomeric human IgA1
    • Furtado P.B., Whitty P.W., Robertson A., Eaton J.T., Almogren A., Kerr M.A., Woof J.M., and Perkins S.J. Solution structure determination of monomeric human IgA2 by X-ray and neutron scattering, analytical ultracentrifugation and constrained modelling: a comparison with monomeric human IgA1. J. Mol. Biol. 338 (2004) 921-941
    • (2004) J. Mol. Biol. , vol.338 , pp. 921-941
    • Furtado, P.B.1    Whitty, P.W.2    Robertson, A.3    Eaton, J.T.4    Almogren, A.5    Kerr, M.A.6    Woof, J.M.7    Perkins, S.J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.