Crystal structures of the human IgD Fab reveal insights into CH1 domain diversity
Copyright © 2023 The Authors. Published by Elsevier Ltd.. All rights reserved..
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.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2023 |
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| Erschienen: |
2023 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:159 |
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| Enthalten in: |
Molecular immunology - 159(2023) vom: 15. Juli, Seite 28-37 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Davies, Anna M [VerfasserIn] |
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| Links: |
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| Themen: |
Antibody |
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| Anmerkungen: |
Date Completed 13.06.2023 Date Revised 03.07.2023 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.molimm.2023.05.006 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM357698665 |
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| 245 | 1 | 0 | |a Crystal structures of the human IgD Fab reveal insights into CH1 domain diversity |
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| 500 | |a Date Revised 03.07.2023 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Copyright © 2023 The Authors. Published by Elsevier Ltd.. All rights reserved. | ||
| 520 | |a 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 | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a Antibody | |
| 650 | 4 | |a C(H)1 domain | |
| 650 | 4 | |a Fab | |
| 650 | 4 | |a IgD | |
| 650 | 4 | |a Immunoglobulin | |
| 650 | 4 | |a X-ray crystallography | |
| 650 | 7 | |a Immunoglobulin Fab Fragments |2 NLM | |
| 650 | 7 | |a Immunoglobulin Isotypes |2 NLM | |
| 700 | 1 | |a Beavil, Rebecca L |e verfasserin |4 aut | |
| 700 | 1 | |a Barbolov, Momchil |e verfasserin |4 aut | |
| 700 | 1 | |a Sandhar, Balraj S |e verfasserin |4 aut | |
| 700 | 1 | |a Gould, Hannah J |e verfasserin |4 aut | |
| 700 | 1 | |a Beavil, Andrew J |e verfasserin |4 aut | |
| 700 | 1 | |a Sutton, Brian J |e verfasserin |4 aut | |
| 700 | 1 | |a McDonnell, James M |e verfasserin |4 aut | |
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