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Crystal Structures of Neuraminidase-Antibody Complexes
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1989
Year
Crystal StructureImmunologyMolecular BiologyAntigen-antibody ComplexesViral Structural ProteinVirus StructureProtein FoldingProtein X-ray CrystallographyAntibody EngineeringFabs Nc41BiophysicsAntigen-antibody InteractionsVirologyAntibody ScreeningCrystallographyStructural BiologyNatural SciencesCrystal StructuresProtein EngineeringInfluenza VaccineMedicine
The nature of antigen-antibody interactions has become clearer in the last few years as crystal structures of antigen-antibody complexes have been elucidated. Such structures have permitted a visualization of the interface between antigen and antibody. Three-dimensional structures of five complexes have now been reported, two containing the influenza virus neuraminidase as antigen and the Fabs NC41 and NC10 (Colman et al. 1987, 1989), and three with hen egg-white lysozyme and the Fabs D1.3, HyHEL-5, and HyHEL-10 (Amit et al. 1986; Sheriff et al. 1987b; E.A. Padlan et al., in prep.). The major parameters that define the scope of the antigen-antibody interface are emerging as more structures are solved and refined to greater precision. Several reviews have dealt with this topic (Mariuzza et al. 1987; Colman 1988; Davies et al. 1988).