Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5549
pubmed:dateCreated
2001-12-13
pubmed:databankReference
pubmed:abstractText
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:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Acetylglucosamine, http://linkedlifedata.com/resource/pubmed/chemical/CLEC4M protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Calcium, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules, http://linkedlifedata.com/resource/pubmed/chemical/Collectins, http://linkedlifedata.com/resource/pubmed/chemical/DC-specific ICAM-3 grabbing..., http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/HIV Envelope Protein gp120, http://linkedlifedata.com/resource/pubmed/chemical/Lectins, http://linkedlifedata.com/resource/pubmed/chemical/Lectins, C-Type, http://linkedlifedata.com/resource/pubmed/chemical/Ligands, http://linkedlifedata.com/resource/pubmed/chemical/Mannose, http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
294
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2163-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11739956-Acetylglucosamine, pubmed-meshheading:11739956-Calcium, pubmed-meshheading:11739956-Carbohydrate Conformation, pubmed-meshheading:11739956-Carbohydrate Sequence, pubmed-meshheading:11739956-Carrier Proteins, pubmed-meshheading:11739956-Cell Adhesion Molecules, pubmed-meshheading:11739956-Collectins, pubmed-meshheading:11739956-Crystallization, pubmed-meshheading:11739956-Crystallography, X-Ray, pubmed-meshheading:11739956-Glycoproteins, pubmed-meshheading:11739956-HIV Envelope Protein gp120, pubmed-meshheading:11739956-Humans, pubmed-meshheading:11739956-Hydrogen Bonding, pubmed-meshheading:11739956-Lectins, pubmed-meshheading:11739956-Lectins, C-Type, pubmed-meshheading:11739956-Ligands, pubmed-meshheading:11739956-Mannose, pubmed-meshheading:11739956-Models, Molecular, pubmed-meshheading:11739956-Molecular Sequence Data, pubmed-meshheading:11739956-Oligosaccharides, pubmed-meshheading:11739956-Protein Conformation, pubmed-meshheading:11739956-Protein Folding, pubmed-meshheading:11739956-Protein Structure, Secondary, pubmed-meshheading:11739956-Receptors, Cell Surface
pubmed:year
2001
pubmed:articleTitle
Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR.
pubmed:affiliation
Department of Structural Biology, University School of Medicine, Stanford, CA 94305, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't