Structures of bacterial immunoglobulin-binding domains and their complexes with immunoglobulins.
Three-dimensional structures are now available for several immunoglobulin binding domains from bacterial proteins A, G, and L. X-ray diffraction and NMR experiments on complexes of these domains with portions of immunoglobulins have revealed common structural themes used in these interactions. These data expand our understanding of structure/function relationships in these molecular recognition processes and provide the basis for rational design of artificial immunoglobulin-binding molecules.
Center for Advanced Biotechnology and Medicine, Rutgers University, Piscataway, USA.
M
M
Tashiro
G T
GT
Montelione
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D001666:Binding Sites, Antibody; D007128:Immunoglobulin Fragments / Q000737:chemistry; D008969:Molecular Sequence Data; D013205:Staphylococcal Protein A / Q000737:chemistry
D001426:Bacterial Proteins; C055047:Ig L-binding protein, Peptostreptococcus; C034284:IgG Fc-binding protein, Streptococcus; D007128:Immunoglobulin Fragments; D013205:Staphylococcal Protein A