Structural highlights
Publication Abstract from PubMed
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 A. These IgD Fab crystals provide the first high-resolution views of the unique Cdelta1 domain. Structural comparisons identify regions of conformational diversity within the Cdelta1 domain, as well as among the homologous domains of Calpha1, Cgamma1 and Cmu1. 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.
Crystal structures of the human IgD Fab reveal insights into C(H)1 domain diversity.,Davies AM, Beavil RL, Barbolov M, Sandhar BS, Gould HJ, Beavil AJ, Sutton BJ, McDonnell JM Mol Immunol. 2023 Jul;159:28-37. doi: 10.1016/j.molimm.2023.05.006. Epub 2023 Jun , 1. PMID:37267832[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Davies AM, Beavil RL, Barbolov M, Sandhar BS, Gould HJ, Beavil AJ, Sutton BJ, McDonnell JM. Crystal structures of the human IgD Fab reveal insights into C(H)1 domain diversity. Mol Immunol. 2023 Jul;159:28-37. PMID:37267832 doi:10.1016/j.molimm.2023.05.006
