ArticleJournal of molecular biology2009
Autonomous tetramerization domains in the glycan-binding receptors DC-SIGN and DC-SIGNR.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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Who cites it
19 citing papers in PubMed, 36 citations in OpenAlex.
- Beyond the Toll-Like Receptor 4. Structure-Dependent Lipopolysaccharide Recognition Systems: How far are we?ChemMedChem · 2025Review
- From structure to function - Ligand recognition by myeloid C-type lectin receptors.Computational and structural biotechnology journal · 2022Review
- DC-SIGN binding to mannosylated B-cell receptors in follicular lymphoma down-modulates receptor signaling capacity.Scientific reports · 2021Article
- C-type Lectin CD209L/L-SIGN and CD209/DC-SIGN: Cell Adhesion Molecules Turned to Pathogen Recognition Receptors.Biology · 2020Review
- Molecular Recognition in C-Type Lectins: The Cases of DC-SIGN, Langerin, MGL, and L-Sectin.Chembiochem : a European journal of chemical biology · 2020Review
- C-Type Lectin Receptors in Host Defense Against Bacterial Pathogens.Frontiers in cellular and infection microbiology · 2020Review
- Fine Mapping the Interaction Between Dendritic Cell-Specific Intercellular Adhesion Molecule (ICAM)-3-Grabbing Nonintegrin and the Cytomegalovirus Envelope Glycoprotein B.The Journal of infectious diseases · 2018Article
- Oligomerization domains in the glycan-binding receptors DC-SIGN and DC-SIGNR: Sequence variation and stability differences.Protein science : a publication of the Protein Society · 2017Article
- Nanoclustering as a dominant feature of plasma membrane organization.Journal of cell science · 2014Review
- Structural characterization of the DC-SIGN-Lewis(X) complex.Biochemistry · 2014Article
- Low copy numbers of DC-SIGN in cell membrane microdomains: implications for structure and function.Traffic (Copenhagen, Denmark) · 2014Article
- Solution NMR analyses of the C-type carbohydrate recognition domain of DC-SIGNR protein reveal different binding modes for HIV-derived oligosaccharides and smaller glycan fragments.The Journal of biological chemistry · 2013Article
- Organization of the extracellular portion of the macrophage galactose receptor: a trimeric cluster of simple binding sites for N-acetylgalactosamine.Glycobiology · 2013Article
- The neck region of the C-type lectin DC-SIGN regulates its surface spatiotemporal organization and virus-binding capacity on antigen-presenting cells.The Journal of biological chemistry · 2012Article
- The formation and stability of DC-SIGN microdomains require its extracellular moiety.Traffic (Copenhagen, Denmark) · 2012Article
- Super-resolution imaging of C-type lectin and influenza hemagglutinin nanodomains on plasma membranes using blink microscopy.Biophysical journal · 2012Article
- Geometry and adhesion of extracellular domains of DC-SIGNR neck length variants analyzed by force-distance measurements.Biochemistry · 2011Article
- DC-SIGN and influenza hemagglutinin dynamics in plasma membrane microdomains are markedly different.Biophysical journal · 2011Article
- Segmented helical structure of the neck region of the glycan-binding receptor DC-SIGNR.Journal of molecular biology · 2009Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Multivalent binding of glycans on pathogens and on mammalian cells by the receptors DC-SIGN (CD209) and DC-SIGNR (L-SIGN, CD299) is dependent on correct disposition of the C-type carbohydrate-recognition domains projected at the C-terminal ends of necks at the cell surface. In the work reported here, neck domains of DC-SIGN and DC-SIGNR expressed in isolation are shown to form tetramers in the absence of the CRDs. Stability analysis indicates that interactions between the neck domains account fully for the stability of the tetrameric extracellular portions of the receptors. The neck domains are approximately 40% alpha-helical based on circular dichroism analysis. However, in contrast to other glycan-binding receptors in which fully helical neck regions are intimately associated with C-terminal C-type CRDs, the neck domains in DC-SIGN and DC-SIGNR act as autonomous tetramerization domains and the neck domains and CRDs are organized independently. Neck domains from polymorphic forms of DC-SIGNR that lack some of the repeat sequences show modestly reduced stability, but differences near the C-terminal end of the neck domains lead to significantly enhanced stability of DC-SIGNR tetramers compared to DC-SIGN.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.