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- W232542580 abstract "Publisher Summary Some species of pathogenic bacteria, notably Streptococci and Staphylococci , have proteins on their surface, which bind immunoglobulins, such as protein A from Staph. aureus and protein G from species of Streptococci . This chapter describes the interaction between domain II of protein G and both Fab and Fc in solution by heteronuclear nmr methods, allowing a direct comparison both of the binding of protein G and protein A to Fc, and of the binding of protein G to Fab and Fc. Protein A contains five highly homologous domains, which bind to the Fc portion of immunoglobulin G (IgG), while protein G has three 55-residue IgG-binding domains, which have a broader specificity than protein A for IgGs from different sources. The interactions of the bacterial antibody-binding proteins with their target immunoglobulins involve a very versatile set of protein-protein interactions. The binding sites for both protein A and protein G lie between the C H 2 and C H 3 domains of Fc, overlapping extensively. This interaction involves two a-helices of protein A and the α-helix and one strand of the β-sheet of protein G." @default.
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- W232542580 date "1995-01-01" @default.
- W232542580 modified "2023-09-25" @default.
- W232542580 title "Interactions of bacterial cell-surface proteins with antibodies: a ersatile set of protein-protein interactions" @default.
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- W232542580 doi "https://doi.org/10.1016/s1080-8914(06)80050-5" @default.
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