Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2007-2-12
pubmed:abstractText
Natural killer (NK) cells are lymphocytes of the innate immune system specialized in recognition and killing of certain virus-infected and tumor cells. To carry out this task, NK cells are equipped with a complex array of germ line encoded receptors. These receptors deliver either positive or negative signals, and a delicate balance between these signals governs the NK cell cytolytic activity against the target cell. IRp60 (CD300a) is a human NK inhibitory receptor with an immunoglobulin-like fold. In the present study the IRp60 protein was expressed in Escherichia coli as inclusion bodies and refolded by dilution. The refolded protein was purified to homogeneity, biochemical characterized and the solution structure was investigated using small-angle X-ray scattering (SAXS). The SAXS data revealed that IRp60 is monomeric in solution with a molecular shape characteristic of the immunoglobulin-like structures. A homology model of IRp60 was built and validated experimentally against the SAXS data.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0141-8130
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
193-200
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Molecular analysis and solution structure from small-angle X-ray scattering of the human natural killer inhibitory receptor IRp60 (CD300a).
pubmed:affiliation
Laboratorio di Medicina Molecolare, Istituto Giannina Gaslini, Largo Gerolamo Gaslini 5, 16147 Genova, Italy. ndimasi@gmail.com
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't