Cryomicroscopy reveals the structural basis for a flexible hinge motion in the immunoglobulin M pent...
Cryomicroscopy reveals the structural basis for a flexible hinge motion in the immunoglobulin M pentamer
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London: Nature Publishing Group UK
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English
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London: Nature Publishing Group UK
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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...
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Cryomicroscopy reveals the structural basis for a flexible hinge motion in the immunoglobulin M pentamer
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TN_cdi_doaj_primary_oai_doaj_org_article_7962a80d2bbe4a1fad840d8055778419
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_7962a80d2bbe4a1fad840d8055778419
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ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-022-34090-2
