Naturally processed peptides from two disease-resistance-associated HLA-DR13 alleles show related sequence motifs and the effects of the dimorphism at position 86 of the HLA-DR beta chain.

doi:10.1073/pnas.92.14.6567

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Article

Naturally processed peptides from two disease-resistance-associated HLA-DR13 alleles show related sequence motifs and the effects of the dimorphism at position 86 of the HLA-DR beta chain.

Proceedings of the National Academy of Sciences of the United States of America - 3 Jul 1995

Davenport M P, Quinn C L, Chicz R M, Green B N, Willis A C, Lane W S, Bell J I, Hill A V

Abstract excerpt

HLA-DR13 has been associated with resistance to two major infectious diseases of humans. To investigate the peptide binding specificity of two HLA-DR13 molecules and the effects of the Gly/Val dimorphism at position 86 of the HLA-DR beta chain on natural peptide ligands, these peptides were acid-eluted from immunoaffinity-purified HLA-DRB1*1301 and -DRB1*1302, molecules that differ only at this position. The...

Topics

Alleles
Amino Acid Sequence
B-Lymphocytes
Cell Line, Transformed
Disease Susceptibility
Gas Chromatography-Mass Spectrometry
Genes, MHC Class II
Genetic Predisposition to Disease
HLA-DR Antigens

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

HLA-DRB1 Chains

Humans

Macromolecular Substances

Molecular Sequence Data

Peptide Fragments

Sequence Homology, Amino Acid

Source

Open in PubMed Open full text

Identifiers

PMID: 7604034
DOI: 10.1073/pnas.92.14.6567
PMCID: PMC41559

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7604034-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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