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PDBsum entry 1for
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Immunoglobulin
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PDB id
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1for
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure determination of an FAB fragment that neutralizes human rhinovirus 14 and analysis of the FAB-Virus complex.
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Authors
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H.Liu,
T.J.Smith,
W.M.Lee,
A.G.Mosser,
R.R.Rueckert,
N.H.Olson,
R.H.Cheng,
T.S.Baker.
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Ref.
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J Mol Biol, 1994,
240,
127-137.
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PubMed id
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Abstract
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The crystal structure of Fab17-IA, an antigen-binding fragment from a murine
immunoglobulin that neutralizes human rhinovirus 14 (HRV14), has been solved to
2.7 A resolution. Fab17-IA crystallized into three different space groups
depending upon the method used to purify the intact antibody. The structure was
determined by use of molecular and isomorphous replacement methods. The current
model has a crystallographic R-factor of approximately 19% for 10,192
independent reflections between 8 and 2.7 A. Correlation coefficient
calculations showed that the Fab17-IA structure can be fit into the
Fab17-IA/HRV14 image reconstruction density to within 5 A positional accuracy
and to within a few degrees of rotation. The resulting interface of the docked
antibody was examined and showed extensive charge and shape complementarity with
the virus surface that was supported by site-directed mutagenesis experiments.
The success of this approach validates the utility of combining X-ray
crystallography with cryo-electron microscopy of complex macromolecular
assemblies.
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Secondary reference #1
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Title
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Structure of human rhinovirus complexed with FAB fragments from a neutralizing antibody.
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Authors
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T.J.Smith,
N.H.Olson,
R.H.Cheng,
H.Liu,
E.S.Chase,
W.M.Lee,
D.M.Leippe,
A.G.Mosser,
R.R.Rueckert,
T.S.Baker.
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Ref.
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J Virol, 1993,
67,
1148-1158.
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PubMed id
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Secondary reference #2
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Title
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Structure of a human rhinovirus-Bivalently bound antibody complex: implications for viral neutralization and antibody flexibility.
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Authors
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T.J.Smith,
N.H.Olson,
R.H.Cheng,
E.S.Chase,
T.S.Baker.
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Ref.
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Proc Natl Acad Sci U S A, 1993,
90,
7015-7018.
[DOI no: ]
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PubMed id
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