Structural basis for antigen recognition by methylated lysine-specific antibodies.
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ABSTRACT: Proteins are modulated by a variety of posttranslational modifications including methylation. Despite its importance, the majority of protein methylation modifications discovered by mass spectrometric analyses are functionally uncharacterized, partly owing to the difficulty in obtaining reliable methylsite-specific antibodies. To elucidate how functional methylsite-specific antibodies recognize the antigens and lead to the development of a novel method to create such antibodies, we use an immunized library paired with phage display to create rabbit monoclonal antibodies recognizing trimethylated Lys260 of MAP3K2 as a representative substrate. We isolated several methylsite-specific antibodies that contained unique complementarity determining region sequence. We characterized the mode of an
SUBMITTER: Ishii M
PROVIDER: S-EPMC7948472 | biostudies-literature | 2021 Jan-Jun
REPOSITORIES: biostudies-literature
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