ArticleJournal of molecular biology2009
Segmented helical structure of the neck region of the glycan-binding receptor 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 16 papers.
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Who cites it
16 citing papers in PubMed.
- Covalent Activation of the C-type Lectin DC-SIGN.Angewandte Chemie (International ed. in English) · 2026Article
- Powerful Avidity with a Limited Valency for Virus-Attachment Blockers on DC-SIGN: Combining Chelation and Statistical Rebinding with Structural Plasticity of the Receptor.ACS central science · 2023Article
- DC-SIGN targets amphotericin B-loaded liposomes to diverse pathogenic fungi.Fungal biology and biotechnology · 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
- TETRALEC, Artificial Tetrameric Lectins: A Tool to Screen Ligand and Pathogen Interactions.International journal of molecular sciences · 2020Article
- Identification of a secondary binding site in human macrophage galactose-type lectin by microarray studies: Implications for the molecular recognition of its ligands.The Journal of biological chemistry · 2019Article
- N-glycan mediated adhesion strengthening during pathogen-receptor binding revealed by cell-cell force spectroscopy.Scientific reports · 2017Article
- 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
- Recent insights into structures and functions of C-type lectins in the immune system.Current opinion in structural biology · 2015Review
- Alteration of the langerin oligomerization state affects Birbeck granule formation.Biophysical journal · 2015Article
- Organization of the extracellular portion of the macrophage galactose receptor: a trimeric cluster of simple binding sites for N-acetylgalactosamine.Glycobiology · 2013Article
- Article
- Virus entry: old viruses, new receptors.Current opinion in virology · 2012Review
- Geometry and adhesion of extracellular domains of DC-SIGNR neck length variants analyzed by force-distance measurements.Biochemistry · 2011Article
- Identification of novel contributions to high-affinity glycoprotein-receptor interactions using engineered ligands.Journal of molecular biology · 2010Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Carbohydrate-recognition domains (CRDs) in the glycan-binding receptors DC-SIGN (dendritic-cell-specific intercellular adhesion molecule 1-grabbing nonintegrin; CD209) and DC-SIGNR (DC-SIGN-related receptor, also known as L-SIGN and variously designated CD209L and CD299) are projected from the membrane surface by extended neck domains containing multiple repeats of a largely conserved 23-amino-acid sequence motif. Crystals of a fragment of the neck domain of DC-SIGNR containing multiple repeats in which each molecule extends through multiple unit cells, such that the observed crystallographic asymmetric unit represents one repeat averaged over six repeats of the protein, have been obtained. The repeats are largely alpha-helical. Based on the structure and arrangement of the repeats in the crystal, the neck region can be described as a series of four-helix bundles connected by short, non-helical linkers. Combining the structure of the isolated neck domain with a previously determined overlapping structure of the distal end of the neck region with the CRDs attached provides a model of the almost-complete extracellular portion of the receptor. The results are consistent with previous characterization of the extended structure for the isolated neck region and the extracellular domain. The organization of the neck suggests how CRDs may be disposed differently in DC-SIGN compared with DC-SIGNR and in variant forms of DC-SIGNR assembled from polypeptides with different numbers of repeats in the neck domain.
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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.