Linked Life Data

9010926

Source:http://linkedlifedata.com/resource/pubmed/id/9010926

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1997-4-1
pubmed:abstractText
Following a recent model of human interleukin-7 (IL-7), we present here a modeling study of the extracellular part of the human IL-7 receptor complex, including the IL-7 specific (IL-7R) and the common gamma (gamma c) chains. The investigation is based on structural homology to the complex of human growth hormone (hGH) bound to its receptor (hGHR). For domain 1 of IL-7R two different models are presented which differ in the alignment to hGHR in three regions. However, these differences affect binding to IL-7 in only one region, at the interface between loop EF of domain 1 of IL-7R and helix C of IL-7. The disulfide pattern in domain 1 of IL-7R is predicted to deviate from that observed in hGHR in that the C'-E disulfide (hGHR) is replaced by a C-C' cross-link. The prediction for the gamma c chain is compared with two previous studies. The models of the complex provide insight into the binding of IL-7 to its receptor and have implications for the suggestion of mutagenesis experiments and the design of (ant)agonists.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0269-2139
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1135-42
pubmed:dateRevised
2009-9-29
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Homology modeling study of the human interleukin-7 receptor complex.
pubmed:affiliation
Physical and Theoretical Chemistry Laboratory, University of Oxford, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't