Linked Life Data

8318453

Source:http://linkedlifedata.com/resource/pubmed/id/8318453

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1993-8-5
pubmed:abstractText
The derived amino acid sequence of the human TCR beta chain shows considerable homology to lg lambda light chains in its variable (V) and constant (C) domains, and in its joining segment (J). We assessed the cross-reactivity between TCR beta chains and lg light chains by synthesizing a set of nested, overlapping 16-mer peptides that duplicated the sequence that corresponds to the continuous VDJC sequence of TCR beta chain and determining the capacity of rabbit antisera to human or murine lgs to react with these peptides. The reactivities we observed were consistent with homologies to lambda and kappa light chains. The strongest reactivity in ELISA binding and competitive inhibition was with a peptide that corresponds to the 'switch peptide' of light chains. The sequence is encoded by the C-terminal region of the J segment (Fr4) and the N-terminus of the C region. Other regions reactive with anti-light chain sera corresponded respectively to CDR1 and Fr3 segments of the V region, and a segment of the constant region predicted to loop out of the tight globular structure. The peptide immunochemical results, coupled with the identification of specific regions of sequence correspondence between TCR beta and the characterized lambda light chain Mcg, allowed us to develop a three-dimensional model of the beta chain consistent with its role in antigen recognition and response to superantigens.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0953-8178
pubmed:author
pubmed:issnType
Print
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
491-502
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Reactions of anti-immunoglobulin sera with synthetic T cell receptor peptides: implications for the three-dimensional structure and function of the TCR beta chain.
pubmed:affiliation
Department of Microbiology and Immunology, University of Arizona, College of Medicine, Tucson 85724.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.