dc.contributor.author | Davies, AM | |
dc.contributor.author | Beavil, RL | |
dc.contributor.author | Barbolov, M | |
dc.contributor.author | Sandhar, BS | |
dc.contributor.author | Gould, HJ | |
dc.contributor.author | Beavil, AJ | |
dc.contributor.author | Sutton, BJ | |
dc.contributor.author | McDonnell, JM | |
dc.date.accessioned | 2024-05-13T14:08:10Z | |
dc.date.available | 2023-05-20 | |
dc.date.available | 2024-05-13T14:08:10Z | |
dc.date.issued | 2023-06-01 | |
dc.identifier.citation | Anna M. Davies, Rebecca L. Beavil, Momchil Barbolov, Balraj S. Sandhar, Hannah J. Gould, Andrew J. Beavil, Brian J. Sutton, James M. McDonnell, Crystal structures of the human IgD Fab reveal insights into CH1 domain diversity, Molecular Immunology, Volume 159, 2023, Pages 28-37, ISSN 0161-5890, https://doi.org/10.1016/j.molimm.2023.05.006. (https://www.sciencedirect.com/science/article/pii/S0161589023001013) Abstract: Antibodies of the IgD isotype remain the least well characterized of the mammalian immunoglobulin isotypes. Here we report three-dimensional structures for the Fab region of IgD, based on four different crystal structures, at resolutions of 1.45–2.75 Å. These IgD Fab crystals provide the first high-resolution views of the unique Cδ1 domain. Structural comparisons identify regions of conformational diversity within the Cδ1 domain, as well as among the homologous domains of Cα1, Cγ1 and Cμ1. The IgD Fab structure also possesses a unique conformation of the upper hinge region, which may contribute to the overall disposition of the very long linker sequence between the Fab and Fc regions found in human IgD. Structural similarities observed between IgD and IgG, and differences with IgA and IgM, are consistent with predicted evolutionary relationships for the mammalian antibody isotypes. Keywords: IgD; CH1 domain; Fab; Antibody; Immunoglobulin; X-ray crystallography | en_US |
dc.identifier.issn | 0161-5890 | |
dc.identifier.uri | https://qmro.qmul.ac.uk/xmlui/handle/123456789/96845 | |
dc.description.abstract | Antibodies of the IgD isotype remain the least well characterized of the mammalian immunoglobulin isotypes. Here we report three-dimensional structures for the Fab region of IgD, based on four different crystal structures, at resolutions of 1.45–2.75 Å. These IgD Fab crystals provide the first high-resolution views of the unique Cδ1 domain. Structural comparisons identify regions of conformational diversity within the Cδ1 domain, as well as among the homologous domains of Cα1, Cγ1 and Cμ1. The IgD Fab structure also possesses a unique conformation of the upper hinge region, which may contribute to the overall disposition of the very long linker sequence between the Fab and Fc regions found in human IgD. Structural similarities observed between IgD and IgG, and differences with IgA and IgM, are consistent with predicted evolutionary relationships for the mammalian antibody isotypes. | en_US |
dc.format.extent | 28 - 37 | |
dc.publisher | Elsevier | en_US |
dc.relation.ispartof | MOLECULAR IMMUNOLOGY | |
dc.rights | Published by Elsevier Ltd. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). | |
dc.subject | IgD | en_US |
dc.subject | CH1 domain | en_US |
dc.subject | Fab | en_US |
dc.subject | Antibody | en_US |
dc.subject | Immunoglobulin | en_US |
dc.subject | X-ray crystallography | en_US |
dc.title | Crystal structures of the human IgD Fab reveal insights into CH1 domain diversity | en_US |
dc.type | Article | en_US |
dc.rights.holder | © 2023 The Author(s). | |
dc.identifier.doi | 10.1016/j.molimm.2023.05.006 | |
pubs.author-url | https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:001012536600001&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=612ae0d773dcbdba3046f6df545e9f6a | en_US |
pubs.notes | Not known | en_US |
pubs.publication-status | Published | en_US |
pubs.volume | 159 | en_US |
rioxxterms.funder | Default funder | en_US |
rioxxterms.identifier.project | Default project | en_US |