1K9I
Complex of DC-SIGN and GlcNAc2Man3
Summary for 1K9I
Entry DOI | 10.2210/pdb1k9i/pdb |
Related | 1k9J |
Descriptor | mDC-SIGN1B type I isoform, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose, CALCIUM ION, ... (4 entities in total) |
Functional Keywords | c-type lectin, protein carbohydrate complex, sugar binding protein |
Biological source | Homo sapiens (human) |
Total number of polymer chains | 10 |
Total formula weight | 183933.05 |
Authors | Feinberg, H.,Mitchell, D.A.,Drickamer, K.,Weis, W.I. (deposition date: 2001-10-29, release date: 2001-12-21, Last modification date: 2024-11-20) |
Primary citation | Feinberg, H.,Mitchell, D.A.,Drickamer, K.,Weis, W.I. Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR. Science, 294:2163-2166, 2001 Cited by PubMed Abstract: 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 promotes viral infection of T cells. Crystal structures of carbohydrate-recognition domains of DC-SIGN and of DC-SIGNR bound to oligosaccharide, in combination with binding studies, reveal that these receptors selectively recognize endogenous high-mannose oligosaccharides and may represent a new avenue for developing HIV prophylactics. PubMed: 11739956DOI: 10.1126/science.1066371 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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