메뉴 건너뛰기




Volumn 2, Issue 8, 1994, Pages 733-746

The structure of a complex between the NC10 antibody and influenza virus neuraminidase and comparison with the overlapping binding site of the NC41 antibody

Author keywords

antibody antigen complex; influenza virus neuraminidase; recognition; structure

Indexed keywords

HN PROTEIN; IMMUNOGLOBULIN F(AB) FRAGMENT; RECOMBINANT PROTEIN; VIRUS ANTIBODY;

EID: 0028774037     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00074-5     Document Type: Article
Times cited : (138)

References (67)
  • 4
    • 0024203268 scopus 로고
    • Structure of antibody –antigen complexes: implications for immune recognition
    • (1988) Adv. Immunol , vol.43 , pp. 99-132
    • Colman1
  • 8
    • 0023432797 scopus 로고
    • Distribution of sequence differences in influenza N9 neuraminidase of tern and whale viruses and crystallization of the whale neuraminidase complexed with antibodies
    • (1987) Virology , vol.160 , pp. 346-354
    • Air1    Webster2    Colman3    Laver4
  • 10
    • 0023226739 scopus 로고
    • Antigenic structure and variation in an influenza N9 neuraminidase
    • (1987) J. Virol , vol.61 , pp. 2910-2916
    • Webster1    Laver2
  • 11
    • 12044252333 scopus 로고
    • Molecular basis of crossreactivity and the limits of antibody––– antigen complementarity
    • (1993) Nature , vol.365 , pp. 859-863
    • Arevalo1    Taussig2    Wilson3
  • 12
    • 0020629047 scopus 로고
    • Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 å resolution
    • (1983) Nature , vol.303 , pp. 35-40
    • Varghese1    Laver2    Colman3
  • 13
    • 0020633096 scopus 로고
    • Structure of the catalytic and antigenic sites in influenza virus neuraminidase
    • (1983) Nature , vol.303 , pp. 41-44
    • Colman1    Varghese2    Laver3
  • 14
    • 0025895628 scopus 로고
    • Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2 å resolution
    • (1991) J. Mol. Biol , vol.221 , pp. 473-486
    • Varghese1    Colman2
  • 15
    • 0025874138 scopus 로고
    • Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants
    • (1991) J. Mol. Biol , vol.221 , pp. 487-497
    • Tulip1    Colman2
  • 17
    • 84911345272 scopus 로고
    • Refined atomic structures of N9 subtype influenza virus neuraminidase: enzyme and escape mutants
    • (1991) J. Mol. Biol , vol.16 , pp. 57-63
    • Malby1    Colman2
  • 18
    • 0028294931 scopus 로고
    • Recombinant anti-sialidase single-chain variable fragment antibody. Characterization, formation of dimer and higher-molecular-mass multimers and the solution of the crystal structure of the single-chain variable fragment/sialidase complex
    • (1994) Eur. J. Biochem , vol.221 , pp. 151-157
    • Kortt1    Colman2
  • 19
    • 0026597444 scopus 로고
    • The free R value: a novel statistical quantity for assessing the accuracy of crystal structures
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger1
  • 20
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la determination des structures cristallines
    • (1952) Acta Crystallographica , vol.5 , pp. 802-810
    • Luzzati1
  • 24
    • 0026631064 scopus 로고
    • Refined crystal structure of a recombinant immunoglobulin domain and a complementarity-determining region 1-grafted mutant
    • (1992) J. Mol. Biol , vol.225 , pp. 739-753
    • Steipe1    Pl ückthun2    Huber3
  • 25
    • 0027299695 scopus 로고
    • Three-dimensional structure of an anti-steroid Fab′ and progesterone–ndash;ndash;ndash; Fab′ complex
    • (1993) J. Mol. Biol , vol.231 , pp. 103-118
    • Arevalo1    Stura2    Taussig3    Wilson4
  • 32
    • 0017411710 scopus 로고
    • The protein data bank: a computer-based archival system for macromolecular structures
    • (1977) J. Mol. Biol , vol.112 , pp. 535-542
    • Bernstein1    Tasumi2
  • 33
    • 0023278330 scopus 로고
    • Canonical structures for the hypervariable regions of immunoglobulins
    • (1987) J. Mol. Biol , vol.196 , pp. 901-917
    • Chothia1    Lesk2
  • 35
    • 0024844388 scopus 로고
    • Conformations of immunoglobulin hypervariable regions
    • (1989) Nature , vol.342 , pp. 877-883
    • Chothia1    Poljak2
  • 39
    • 0025275610 scopus 로고
    • On the nature of antibody combining sites: unusual structural features that may confer on these sites an enhanced capacity for binding ligands
    • (1990) Proteins , vol.7 , pp. 112-124
    • Padlan1
  • 41
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: crystal structure of the complex
    • (1992) Science , vol.255 , pp. 306-312
    • de Vos1    Ultsch2    Kossiakoff3
  • 44
    • 0026757989 scopus 로고
    • Three dimensional structure of an angiotensin II– Fab complex at 3å: hormone recognition by an antiidiotypic antibody
    • (1992) Science , vol.257 , pp. 502-507
    • Garcia1    Ronco2    Verroust3    Br ünger4    Amzel5
  • 47
    • 0024375777 scopus 로고
    • Immune response to a molecularly defined internal image idiotope
    • (1989) J. Immunol , vol.142 , pp. 4392-4400
    • Williams1    Greene2
  • 49
    • 0022637867 scopus 로고
    • Molecular mimicry: frequency of reactivity of monoclonal antiviral antibodies with normal tissues
    • (1986) J. Virol , vol.57 , pp. 397-401
    • Srinivasappa1    Notkins2
  • 50
    • 0023161406 scopus 로고
    • Mutation drift and repertoire shift in the maturation of the immune response
    • (1987) Immunol. Rev , vol.96 , pp. 23-41
    • Berek1    Milstein2
  • 56
    • 0026963905 scopus 로고
    • The Weissenberg method for the collection of X-ray diffraction data from macromolecular crystals: modifications to the data-processing program WEIS
    • (1992) J. Appl. Crystallogr , vol.25 , pp. 809-811
    • Fields1    Guss2    Lawrence3    Nakagawa4
  • 57
    • 0022298619 scopus 로고
    • Constrained-restrained least-squares (CORELS) refinement of proteins and nucleic acids
    • (1985) Methods Enzymol , vol.115 , pp. 271-303
    • Sussman1
  • 58
    • 0022325950 scopus 로고
    • Resolution of phase ambiguity in macromolecular crystallography
    • (1985) Methods Enzymol , vol.115 , pp. 90-112
    • Wang1
  • 65
    • 0018780591 scopus 로고
    • Side-chain torsional potentials: effect of dipeptide, protein, and solvent environment
    • (1979) Biochemistry , vol.18 , pp. 1256-1268
    • Gelin1    Karplus2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.