Structural Basis for Selective Recognition of Oligosaccharides by DC-SIGN and DC-SIGNR

  title={Structural Basis for Selective Recognition of Oligosaccharides by DC-SIGN and DC-SIGNR},
  author={Hadar Feinberg and Daniel Mitchell and Kurt Drickamer and William I. Weis},
  pages={2163 - 2166}
Dendritic cell specific intracellular adhesion molecule–3 (ICAM-3) grabbing nonintegrin (DC-SIGN), a C-type lectin present on the surface of dendritic cells, mediates the initial interaction of dendritic cells with T cells by binding to ICAM-3. DC-SIGN and DC-SIGNR, a related receptor found on the endothelium of liver sinusoids, placental capillaries, and lymph nodes, bind to oligosaccharides that are present on the envelope of human immunodeficiency virus (HIV), an interaction that strongly… 
Structural Characterization of the DC-SIGN–LewisX Complex
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Comparative analysis reveals selective recognition of glycans by the dendritic cell receptors DC-SIGN and Langerin.
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The structure and functions of DC-SIGN and related CTLDs in the recognition of pathogens, the molecular and structural determinants that regulate the interaction with pathogen-associated molecular patterns are focused on.
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Quinoxalinone Inhibitors of the Lectin DC-SIGN.
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It is shown that DC-SIGN, a DC-specific C-type lectin, supports tethering and rolling of DC-sign–positive cells on the vascular ligand ICAM-2 under shear flow, a prerequisite for emigration from blood.
A Dendritic Cell–Specific Intercellular Adhesion Molecule 3–Grabbing Nonintegrin (Dc-Sign)–Related Protein Is Highly Expressed on Human Liver Sinusoidal Endothelial Cells and Promotes HIV-1 Infection
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DC-SIGNR, a DC-SIGN homologue expressed in endothelial cells, binds to human and simian immunodeficiency viruses and activates infection in trans
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