Structure of an antibody combining site by magnetic resonance.
The structure of the combining site of the DNP binding IgA mouse myeloma protein MOPC 315 has been determined by a combination of high resolution nuclear magnetic resonance, electron spin resonance, model building and chemical modifications. This approach yields that general dimensions of the site, its polarity and asymmetry features, the assignment of the DNP-contact residues and their three-dimensional coordinates.
D000818:Animals; D001224:Aspartic Acid; D001666:Binding Sites, Antibody; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004136:Dinitrobenzenes / Q000276:immunology*; D004578:Electron Spin Resonance Spectroscopy; D005998:Glycine / Q000031:analogs & derivatives / Q000378:metabolism; D006241:Haptens; D007070:Immunoglobulin A; D007135:Immunoglobulin Variable Region; D009682:Magnetic Resonance Spectroscopy; D051379:Mice; D008956:Models, Chemical; D008968:Molecular Conformation; D009194:Myeloma Proteins; D009578:Nitrobenzenes / Q000276:immunology*; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D014364:Tryptophan
D004136:Dinitrobenzenes; D006241:Haptens; D007070:Immunoglobulin A; D007135:Immunoglobulin Variable Region; D009194:Myeloma Proteins; D009578:Nitrobenzenes; D001224:Aspartic Acid; D014364:Tryptophan; D005998:Glycine