作者: P.C. Keck , J.S. Huston
DOI: 10.1016/S0006-3495(96)79398-0
关键词: Antibody 、 Chemistry 、 Protein structure 、 Binding site 、 Immunoglobulin Fab Fragments 、 Directionality 、 Antibody Binding Site 、 Peptide sequence 、 Stereochemistry 、 Molecular model
摘要: Molecular modeling studies on antibody Fv regions have been pursued to design a second antigen-binding site (chi-site) in chimeric single-chain (chi sFv) species of about 30 kDa. This analysis has uncovered an architectural basis common many that permits grafting chi-site onto the surface diametrically opposes normal combining site. By using molecular graphics analysis, complementarity-determining CDRs) were defined comprised most CDRs from binding interest. The chain directionality chi was consistent with specific bottom loops sFv, which allowed for overall geometry approximating parent Analysis 10 different crystal structures indicates positions inserting are very highly conserved, as corresponding CDR boundaries results this investigation suggest it should be possible generally apply approach development bispecific BABS) proteins.