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Cryomicroscopy reveals the structural basis for a flexible hinge motion in the immunoglobulin M pentamer

23 Oct 2022

Abstract excerpt

Immunoglobulin M (IgM) is the most ancient of the five isotypes of immunoglobulin (Ig) molecules and serves as the first line of defence against pathogens. Here, we use cryo-EM to image the structure of the human full-length IgM pentamer, revealing antigen binding domains flexibly attached to the asymmetric and rigid core formed by the Cμ4 and Cμ3 constant regions and the J-chain. A hinge is located at the...

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PMID: 36274064
DOI: 10.1038/s41467-022-34090-2

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