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Titolo:
BINDING OF SINGLE SUBSTITUTED PROMISCUOUS AND DESIGNER PEPTIDES TO PURIFIED DRB1-ASTERISK-0101
Autore:
MACKLIN KD; CONTIFINE BM;
Indirizzi:
UNIV MINNESOTA,DEPT BIOCHEM,1479 GORTNER AVE ST PAUL MN 55108 UNIV MINNESOTA,DEPT PHARMACOL MINNEAPOLIS MN 55455
Titolo Testata:
Biochemical and biophysical research communications
fascicolo: 2, volume: 242, anno: 1998,
pagine: 322 - 326
SICI:
0006-291X(1998)242:2<322:BOSSPA>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
CLASS-II MOLECULES; MHC CLASS-II; MUSCLE ACETYLCHOLINE-RECEPTOR; MYASTHENIA-GRAVIS; HLA-DR; HISTOCOMPATIBILITY ANTIGEN; CELL RECOGNITION; GAMMA-SUBUNIT; T-CELLS; HLA-DR1;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
34
Recensione:
Indirizzi per estratti:
Citazione:
K.D. Macklin e B.M. Contifine, "BINDING OF SINGLE SUBSTITUTED PROMISCUOUS AND DESIGNER PEPTIDES TO PURIFIED DRB1-ASTERISK-0101", Biochemical and biophysical research communications, 242(2), 1998, pp. 322-326

Abstract

MIC class II molecules present antigenic peptides to T cells. The sequence characteristics of peptides associated with various class II alleles have been examined by analysis of peptide mixtures extracted frompurified class LT molecules as well by direct binding assays with substituted synthetic peptides and purified class II molecules. Here, in vitro binding assays with purified DRB10101 and glycine substituted analogues of N gamma 321-340 and alanine substituted analogues of TT948-967, universal CD4(+) epitopes of the gamma subunit of the human nicotinic acetylcholine receptor and tetanus toxin, respectively, were able to compete for binding to an extent similar to that of the unsubstituted peptides. Testing whether this is a property of promiscuous, but not allele-specific peptide epitopes, a designer peptide containing the proposed anchor residues Ear binding DRB10101 was used in similar binding assays, As expected, the binding capacity of this designer peptide was much higher than that of the universal epitope peptides. However, substitution of the anchor residues for alanine in the context of this designer peptide did not abrogate binding to DRB10101 and, in fact, enhanced it. Therefore, it appears that for both class II allele-specific and universal epitope peptides, binding is a result of the combinatory effects of a few residues. The individual replacement of these residues with the sterically and electro-statistically neutral residue alanine does not negatively affect binding in the continued presence of other anchor residues. (C) 1998 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/09/20 alle ore 09:21:55