Structure of an antibody-antigen complex: crystal structure of the HyHEL-10 Fab-lysozyme complex
Eduardo A. Padlan,Enid W. Silverton,Steven Sheriff,Gerson H. Cohen,Sandra J. Smith-Gill,David R. Davies +5 more
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The crystal structure of the complex of the anti-lysozyme HyHEL-10 Fab and hen egg white lysozyme has been determined and the antibody-antigen contact mainly involves hydrogen bonds and van der Waals interactions.Abstract:
The crystal structure of the complex of the anti-lysozyme HyHEL-10 Fab and hen egg white lysozyme has been determined to a nominal resolution of 3.0 A. The antigenic determinant (epitope) on the lysozyme is discontinuous, consisting of residues from four different regions of the linear sequence. It consists of the exposed residues of an alpha-helix together with surrounding amino acids. The epitope crosses the active-site cleft and includes a tryptophan located within this cleft. The combining site of the antibody is mostly flat with a protuberance made up of two tyrosines that penetrate the cleft. All six complementarity-determining regions of the Fab contribute at least one residue to the binding; one residue from the framework is also in contact with the lysozyme. The contacting residues on the antibody contain a disproportionate number of aromatic side chains. The antibody-antigen contact mainly involves hydrogen bonds and van der Waals interactions; there is one ion-pair interaction but it is weak.read more
Citations
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The atomic structure of protein-protein recognition sites.
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References
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TL;DR: The role of complementary hydrogen bonding as a determinant of biological specificity has been examined by protein engineering of the tyrosyl-tRNA synthetase and the presence of an unpaired and charged donor or acceptor weakens binding energy.
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The molecular replacement method
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Three-dimensional structure of a complex of antibody with influenza virus neuraminidase.
Peter M. Colman,W. G. Laver,Joseph N. Varghese,A. T. Baker,P.A. Tulloch,Gillian M. Air,R. G. Webster +6 more
TL;DR: The structure of a complex between influenza virus neuraminidase and an antibody displays features inconsistent with the inflexible 'lock and key' model of antigen‐antibody binding.
Journal ArticleDOI
The galactan-binding immunoglobulin Fab J539: an X-ray diffraction study at 2.6-A resolution.
Se Won Suh,Talapady N. Bhat,Manuel A. Navia,Gerson H. Cohen,D. N. Rao,Stuart Rudikoff,David R. Davies +6 more
TL;DR: The crystal structure of the Fab of the galactan‐binding immunoglobulin J539 (a mouse IgA,κ) has been determined at a resolution of approximately 2.6 Å by X‐ray diffraction using the starting model obtained from the real space search described previously.