1SL4

Crystal Structure of DC-SIGN carbohydrate recognition domain complexed with Man4

Summary for 1SL4

• Entry DOI: 10.2210/pdb1sl4/pdb
• Descriptor: mDC-SIGN1B type I isoform, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: dc-sign, c-type lectin, sugar binding protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 18533.39

Authors

Guo, Y.,Feinberg, H.,Conroy, E.,Mitchell, D.A.,Alvarez, R.,Blixt, O.,Taylor, M.E.,Weis, W.I.,Drickamer, K. (deposition date: 2004-03-05, release date: 2004-06-15, Last modification date: 2024-10-16)

Primary citation

Guo, Y.,Feinberg, H.,Conroy, E.,Mitchell, D.A.,Alvarez, R.,Blixt, O.,Taylor, M.E.,Weis, W.I.,Drickamer, K.
Structural basis for distinct ligand-binding and targeting properties of the receptors DC-SIGN and DC-SIGNR
Nat.Struct.Mol.Biol., 11:591-598, 2004

PubMed Abstract: Both the dendritic cell receptor DC-SIGN and the closely related endothelial cell receptor DC-SIGNR bind human immunodeficiency virus and enhance infection. However, biochemical and structural comparison of these receptors now reveals that they have very different physiological functions. By screening an extensive glycan array, we demonstrated that DC-SIGN and DC-SIGNR have distinct ligand-binding properties. Our structural and mutagenesis data explain how both receptors bind high-mannose oligosaccharides on enveloped viruses and why only DC-SIGN binds blood group antigens, including those present on microorganisms. DC-SIGN mediates endocytosis, trafficking as a recycling receptor and releasing ligand at endosomal pH, whereas DC-SIGNR does not release ligand at low pH or mediate endocytosis. Thus, whereas DC-SIGN has dual ligand-binding properties and functions both in adhesion and in endocytosis of pathogens, DC-SIGNR binds a restricted set of ligands and has only the properties of an adhesion receptor.

PubMed: 15195147
DOI: 10.1038/nsmb784

Experimental method

X-RAY DIFFRACTION (1.55 Å)