Linked Life Data

11741958

Source:http://linkedlifedata.com/resource/pubmed/id/11741958

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2002-2-18
pubmed:abstractText
Siglec-7 is a sialic acid-binding lectin recently identified as an inhibitory receptor on natural killer cells. Here we characterize the sugar-binding specificity of Siglec-7 expressed on Chinese hamster ovary cells using polyvalent streptavidin-based glyco-probes. Glyco-probes carrying unique oligosaccharide structures such as GD3 (NeuAc alpha 2,8NeuAc alpha 2,3Gal beta 1,4Glc) and LSTb (Gal beta 1,3[NeuAc alpha 2,6]GlcNAc beta 1,3Gal beta 1,4Glc) oligosaccharides bound to Siglec-7 better than those carrying LSTc (NeuAc alpha 2,6Gal beta 1,4GlcNAc beta 1,3Gal beta 1,4Glc) or GD1a (NeuAc alpha 2,3Gal beta 1,3GalNAc beta 1,4[NeuAc alpha 2,3]Gal beta 1,4Glc) oligosaccharides. In contrast, Siglec-9, which is 84% identical to Siglec-7, did not bind to the GD3 and LSTb probes but did bind to the LSTc and GD1a probes. To identify a region(s) responsible for their difference in binding specificity, we prepared a series of V-set domain chimeras between Siglecs-7 and -9. Substitution of a small region, Asn(70)-Lys(75), of Siglec-7 with the equivalent region of Siglec-9 resulted in loss of Siglec-7-like binding specificity and acquisition of Siglec-9-like binding properties. In comparison, a Siglec-9-based chimera, which contains Asn(70)-Lys(75) with additional amino acids derived from Siglec-7, exhibited Siglec-7-like specificity. These results, combined with molecular modeling, suggest that the C-C' loop in the sugar-binding domain plays a major role in determining the binding specificities of Siglecs-7 and -9.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6324-32
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11741958-Animals, pubmed-meshheading:11741958-Antigens, CD, pubmed-meshheading:11741958-Antigens, Differentiation, Myelomonocytic, pubmed-meshheading:11741958-CHO Cells, pubmed-meshheading:11741958-Carbohydrate Conformation, pubmed-meshheading:11741958-Carbohydrate Sequence, pubmed-meshheading:11741958-Cricetinae, pubmed-meshheading:11741958-Gangliosides, pubmed-meshheading:11741958-Humans, pubmed-meshheading:11741958-Lectins, pubmed-meshheading:11741958-Models, Molecular, pubmed-meshheading:11741958-Molecular Sequence Data, pubmed-meshheading:11741958-Oligosaccharides, pubmed-meshheading:11741958-Protein Conformation, pubmed-meshheading:11741958-Recombinant Proteins, pubmed-meshheading:11741958-Sialic Acids, pubmed-meshheading:11741958-Substrate Specificity, pubmed-meshheading:11741958-Transfection
pubmed:year
2002
pubmed:articleTitle
A small region of the natural killer cell receptor, Siglec-7, is responsible for its preferred binding to alpha 2,8-disialyl and branched alpha 2,6-sialyl residues. A comparison with Siglec-9.
pubmed:affiliation
Glyco-chain Functions Laboratory, Supra-biomolecular System Group, Frontier Research System, RIKEN Institute, Saitama 351-0198, Japan.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't