ArticleThe Journal of biological chemistry
The cryo-EM structure of the endocytic receptor DEC-205.
Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Secondary Sites of the C-type Lectin-Like Fold.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Review
- Hydatid fluid fromFrontiers in cellular and infection microbiology · 2024Article
- Controlling Antigen Fate in Therapeutic Cancer Vaccines by Targeting Dendritic Cell Receptors.Molecular pharmaceutics · 2023Review
- LRP-1 links post-translational modifications to efficient presentation of celiac disease-specific T cell antigens.Cell chemical biology · 2023Article
- Straight to the point: targeted mRNA-delivery to immune cells for improved vaccine design.Frontiers in immunology · 2023Review
- The mannose receptor ligands and the macrophage glycome.Current opinion in structural biology · 2022Review
- Structure of PLA2R reveals presentation of the dominant membranous nephropathy epitope and an immunogenic patch.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Selenoprotein K Is Essential for the Migration and Phagocytosis of Immature Dendritic Cells.Antioxidants (Basel, Switzerland) · 2022Article
- Medicinal chemistry of the myeloid C-type lectin receptors Mincle, Langerin, and DC-SIGN.RSC medicinal chemistry · 2021Review
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DEC-205 (CD205), a member of the macrophage mannose receptor protein family, is the prototypic endocytic receptor of dendritic cells, whose ligands include phosphorothioated cytosine-guanosine oligonucleotides, a motif often seen in bacterial or viral DNA. However, despite growing biological and clinical significance, little is known about the structural arrangement of this receptor or any of its family members. Here, we describe the 3.2 Å cryo-EM structure of human DEC-205, thereby illuminating the structure of the mannose receptor protein family. The DEC-205 monomer forms a compact structure comprising two intercalated rings of C-type lectin-like domains, where the N-terminal cysteine-rich and fibronectin domains reside at the central intersection. We establish a pH-dependent oligomerization pathway forming tetrameric DEC-205 using solution-based techniques and ultimately solved the 4.9 Å cryo-EM structure of the DEC-205 tetramer to identify the unfurling of the second lectin ring which enables tetramer formation. Furthermore, we suggest the relevance of this oligomerization pathway within a cellular setting, whereby cytosine-guanosine binding appeared to disrupt this cell-surface oligomer. Accordingly, we provide insight into the structure and oligomeric assembly of the DEC-205 receptor.
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