Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-1-29
pubmed:abstractText
The extracellular portion of the alpha-subunit of human high-affinity receptor for immunoglobulin-E (IgE), which contains two immunoglobulin (Ig) domains, was modeled on the basis of sequence similarity with antibody domains of known three-dimensional structure. Each receptor domain contains 86 amino acid residues, and both domains were modeled as bilayer structures. In both domains, one layer is made up of three anti-parallel beta-strands and the other of four strands, with the two layers linked by a disulfide bridge. The two domains show significant sequence similarity with each other (22 identities) and with the homologous domains of the murine and rat high-affinity receptors for IgE and the Fc gamma receptors from various species. Two plausible modes of association of the domains were considered: In the first, the two domains were positioned end-to-end, with essentially only longitudinal interactions between them; in the second, the molecule is more bent, with more lateral interactions between the two domains. The models will be useful in the design of protein engineering studies of this and homologous receptors to delineate the site of interaction with ligand. Furthermore, they may lend themselves as possible probes in crystallographic analyses by molecular replacement techniques.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1052-8040
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
129-44
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
A modeling study of the alpha-subunit of human high-affinity receptor for immunoglobulin-E.
pubmed:affiliation
Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't