alexa Identification of the contact surface of a streptococcal protein G domain complexed with a human Fc fragment.


Pharmaceutical Analytical Chemistry: Open Access

Author(s): Gronenborn AM, Clore GM

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Abstract The B1 domain of streptococcal protein G interacts with the C-terminal fragment of the heavy chain of immunoglobulin G (IgGFc). The binding site for the protein G domain on the antibody fragment is in close proximity or overlapping with that determined for staphylococcal protein A. The interaction of the B1 domain with IgGFc was investigated by 1H-15N correlation spectroscopy. The major interaction site on the B1 domain comprises parts of beta-strand 3 as well as the alpha-helix. Comparison with the crystal structure of the protein A/IgGFc complex suggests that the mode of interaction in the two complexes is analogous, despite the lack of sequence or structural similarity between two antibody binding proteins. This article was published in J Mol Biol and referenced in Pharmaceutical Analytical Chemistry: Open Access

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