Within the body, antibodies trigger various defensive responses against antigens such as pathogenic viruses, bacteria, and allergens that have invaded the body. On the other hand, antibodies can be produced specifically for molecules whose structure and function we wish to elucidate, making them an important tool for understanding life functions and disease causes.
Special Appointment Associate Prof. Satoshi Ogasawara, Professor Takeshi Murata et al., in collaboration with the group of Prof. Yukinari Kato and Medical Chemistry Drug Discovery Inc., have elucidated the atomic-level three-dimensional structure of a monoclonal antibody bound to glycopeptide.
This study not only identified the glycopeptide binding site of antibodies for the first time, but also demonstrated that IgG antibodies possess an advantage over other low-molecular-weight binding molecules in recognizing large, three-dimensional epitopes (antigen recognition sites) such as glycopeptides.
The results were published in Biochemical and Biophysical Research Communications on September 10, 2020.
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