Linked Life Data

2534425

Source:http://linkedlifedata.com/resource/pubmed/id/2534425

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1990-5-21
pubmed:abstractText
The major protein constituent of eosinophilic leukocyte granules is a cytotoxic protein that plays a key role in antiparasitic defence mechanisms and immune hypersensitivity reactions. We show here that the protein is homologous with animal lectins; it exhibits greatest similarity to the lectin domain of the low-affinity IgE receptor of lymphocytes. On the basis of homology with lectins the disulphide bond pattern of the protein is predicted. It is proposed that certain cysteines unique to major basic protein are on the surface of the molecule and are involved in forming disulphide-bonded polymers. Homology with IgE receptor raises the possibility that major basic protein may also bind to IgE antibodies. Such an interaction could provide an efficient way of targeting the cytotoxic protein to parasites and allergens recognized by IgE antibodies.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0161-5890
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1151-4
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Homology of cytotoxic protein of eosinophilic leukocytes with IgE receptor Fc epsilon RII: implications for its structure and function.
pubmed:affiliation
Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest.
pubmed:publicationType
Journal Article