Linked Life Data

16406677

Source:http://linkedlifedata.com/resource/pubmed/id/16406677

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2006-5-23
pubmed:abstractText
The leukocyte immunoglobulin-like receptors (LIRs, also known as ILTs, CD85, and LILRs) comprise a family of related immunoregulatory receptors encoded within the leukocyte receptor cluster (LRC) on human chromosome 19. LIRs are transmembrane proteins containing either two or four extracellular immunoglobulin domains, and most family members are expressed predominantly on myeloid cell lineages. Although the inhibitory receptors LIR-1 and LIR-2 are known to bind to a broad range of class I MHC molecules and are thought to play important roles in immune regulation, the majority of LIRs are currently of unknown structure and their ligands remain unidentified. In this study, we describe recombinant production and characterisation of the extracellular portion of LIR-5 (ILT3), a poorly understood inhibitory receptor that transduces tolerising signals to dendritic cells. The two extracellular immunoglobulin domains of LIR-5 were expressed in Escherichia coli to a high level and were found to accumulate in inclusion bodies. Inclusion bodies were purified, solubilised, and receptor then renatured by dilution refolding, with acceptable yields. Size exclusion chromatography and SDS-PAGE analyses confirmed the extracellular portion behaved as a monomer in solution, and purified protein was antibody-reactive. LIR-5 is representative of a subset of LIR receptors that on the basis of structural and sequence comparisons with LIR-1 seem unlikely to bind class I MHC molecules. Successful prokaryotic generation of correctly folded LIR-5 in high levels has implications for production of other LRC receptors and should greatly facilitate attempts to define the structure and ligands of this important regulator of dendritic cell function.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1046-5928
pubmed:author
pubmed:issnType
Print
pubmed:volume
47
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
490-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:16406677-Antigens, CD, pubmed-meshheading:16406677-Chromatography, Gel, pubmed-meshheading:16406677-Dendritic Cells, pubmed-meshheading:16406677-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:16406677-Escherichia coli, pubmed-meshheading:16406677-Genes, MHC Class I, pubmed-meshheading:16406677-Humans, pubmed-meshheading:16406677-Immune Tolerance, pubmed-meshheading:16406677-Ligands, pubmed-meshheading:16406677-Multigene Family, pubmed-meshheading:16406677-Protein Binding, pubmed-meshheading:16406677-Protein Folding, pubmed-meshheading:16406677-Protein Structure, Tertiary, pubmed-meshheading:16406677-Receptors, Immunologic, pubmed-meshheading:16406677-Recombinant Proteins, pubmed-meshheading:16406677-Signal Transduction, pubmed-meshheading:16406677-Structural Homology, Protein, pubmed-meshheading:16406677-Surface Plasmon Resonance
pubmed:year
2006
pubmed:articleTitle
Expression, purification, and refolding of the myeloid inhibitory receptor leukocyte immunoglobulin-like receptor-5 for structural and ligand identification studies.
pubmed:affiliation
Cancer Research UK Institute for Cancer Studies, University of Birmingham, Edgbaston, UK.
pubmed:publicationType
Journal Article, Comparative Study