Linked Life Data

8416946

Source:http://linkedlifedata.com/resource/pubmed/id/8416946

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1993-1-28
pubmed:abstractText
The mannose receptor of macrophage and hepatic endothelial cells discriminates between endogenous and exogenous sugar-bearing structures. Previous competition studies have indicated that the receptor binds the monosaccharides mannose, fucose, and N-acetylglucosamine but displays much higher affinity for multivalent oligosaccharides, such as those found on the surface of potentially pathogenic microorganisms. The hydrodynamic properties of the receptor have been examined, revealing that the receptor is a monomer. This result suggests that multiple carbohydrate recognition domains (CRDs) in the extracellular domain of a single receptor polypeptide cooperate to achieve high affinity binding of complex ligands. In order to determine the importance of individual CRDs, properties of receptor segments containing groups of CRDs expressed in insect cells have been examined. The results indicate that two of the CRDs (4 and 5) form a protease-resistant, ligand-binding core but that five CRDs in tandem (4-8) are required to match the affinity of the intact receptor for yeast mannan. A consequence of the organization of the receptor is that both valency and geometry of glycoconjugates are important determinants of binding affinity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
399-404
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Structural requirements for high affinity binding of complex ligands by the macrophage mannose receptor.
pubmed:affiliation
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't