Cryomicroscopy reveals the structural basis for a flexible hinge motion in the immunoglobulin M pentamer
Immunoglobulin M (IgM) is the Ig isotype that serves as the first line of host defence during infection. Here, the authors image the full-length IgM pentamer by cryo-EM, revealing the structure and hinge motion of the antigen binding domains.
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2022-10-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-022-34090-2 |
| _version_ | 1798028534684319744 |
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| author | Qu Chen Rajesh Menon Lesley J. Calder Pavel Tolar Peter B. Rosenthal |
| author_facet | Qu Chen Rajesh Menon Lesley J. Calder Pavel Tolar Peter B. Rosenthal |
| author_sort | Qu Chen |
| collection | DOAJ |
| description | Immunoglobulin M (IgM) is the Ig isotype that serves as the first line of host defence during infection. Here, the authors image the full-length IgM pentamer by cryo-EM, revealing the structure and hinge motion of the antigen binding domains. |
| first_indexed | 2024-04-11T19:09:52Z |
| format | Article |
| id | doaj.art-7962a80d2bbe4a1fad840d8055778419 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-04-11T19:09:52Z |
| publishDate | 2022-10-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-7962a80d2bbe4a1fad840d80557784192022-12-22T04:07:39ZengNature PortfolioNature Communications2041-17232022-10-0113111110.1038/s41467-022-34090-2Cryomicroscopy reveals the structural basis for a flexible hinge motion in the immunoglobulin M pentamerQu Chen0Rajesh Menon1Lesley J. Calder2Pavel Tolar3Peter B. Rosenthal4Structural Biology Science Technology Platform, The Francis Crick InstituteImmune Receptor Activation Laboratory, The Francis Crick InstituteStructural Biology of Cells and Viruses Laboratory, The Francis Crick InstituteImmune Receptor Activation Laboratory, The Francis Crick InstituteStructural Biology of Cells and Viruses Laboratory, The Francis Crick InstituteImmunoglobulin M (IgM) is the Ig isotype that serves as the first line of host defence during infection. Here, the authors image the full-length IgM pentamer by cryo-EM, revealing the structure and hinge motion of the antigen binding domains.https://doi.org/10.1038/s41467-022-34090-2 |
| spellingShingle | Qu Chen Rajesh Menon Lesley J. Calder Pavel Tolar Peter B. Rosenthal Cryomicroscopy reveals the structural basis for a flexible hinge motion in the immunoglobulin M pentamer Nature Communications |
| title | Cryomicroscopy reveals the structural basis for a flexible hinge motion in the immunoglobulin M pentamer |
| title_full | Cryomicroscopy reveals the structural basis for a flexible hinge motion in the immunoglobulin M pentamer |
| title_fullStr | Cryomicroscopy reveals the structural basis for a flexible hinge motion in the immunoglobulin M pentamer |
| title_full_unstemmed | Cryomicroscopy reveals the structural basis for a flexible hinge motion in the immunoglobulin M pentamer |
| title_short | Cryomicroscopy reveals the structural basis for a flexible hinge motion in the immunoglobulin M pentamer |
| title_sort | cryomicroscopy reveals the structural basis for a flexible hinge motion in the immunoglobulin m pentamer |
| url | https://doi.org/10.1038/s41467-022-34090-2 |
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