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Article

Distinct conformations of a peptide bound to HLA-DR1 or DRB5*0101 suggested by molecular modelling.

International immunology - 1 Nov 1996

Jurcevic S, Travers P J, Hills A, Agrewala J N, Moreno C, Ivanyi J

Abstract excerpt

The conformation of peptides when bound to different HLA class II molecules is of interest in the study of specificity and function of responding T cells. Here, we report the investigation of the HLA-DR binding profiles of an immunodominant and HLA-promiscuous mycobacterial peptide, p38G. Its binding affinities were found to be high for DR1, moderate for DR2, DR7 and DR8, low for DR4, DR5, DR6 and DR9, and below...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 8943576
DOI: 10.1093/intimm/8.11.1807

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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