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PDBsum entry 1for

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Immunoglobulin PDB id
1for
Contents
Protein chains
210 a.a. *
219 a.a. *
Waters ×157
* Residue conservation analysis

References listed in PDB file
Key reference
Title Structure determination of an FAB fragment that neutralizes human rhinovirus 14 and analysis of the FAB-Virus complex.
Authors H.Liu, T.J.Smith, W.M.Lee, A.G.Mosser, R.R.Rueckert, N.H.Olson, R.H.Cheng, T.S.Baker.
Ref. J Mol Biol, 1994, 240, 127-137.
PubMed id 8027997
Abstract
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.
Secondary reference #1
Title Structure of human rhinovirus complexed with FAB fragments from a neutralizing antibody.
Authors 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.
Ref. J Virol, 1993, 67, 1148-1158.
PubMed id 7679742
Abstract
Secondary reference #2
Title Structure of a human rhinovirus-Bivalently bound antibody complex: implications for viral neutralization and antibody flexibility.
Authors T.J.Smith, N.H.Olson, R.H.Cheng, E.S.Chase, T.S.Baker.
Ref. Proc Natl Acad Sci U S A, 1993, 90, 7015-7018. [DOI no: 10.1073/pnas.90.15.7015]
PubMed id 8394005
Full text Abstract
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