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Article

Possible association of non-binding of HSP70 to HLA-DRB1 peptide sequences and protection from rheumatoid arthritis.

Immunogenetics - 1 May 2002

Maier Jan T, Haug Markus, Föll Jürgen L, Beck Hermann, Kalbacher Hubert, Rammensee Hans-Georg, Dannecker Günther E

Abstract excerpt

The beta-chains of HLA-DR molecules associated with susceptibility to rheumatoid arthritis (RA) share a common amino acid sequence in their third hypervariable region at position 70-74. This shared epitope could either contribute to preferential binding of a given disease-associated peptide, be involved in disease-induction by molecular mimicry or, by binding to heat shock proteins, influence antigen...

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Share to Arthritis, Rheumatoid
Share to Binding Sites

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli Proteins

Share to HLA-DR Antigens

Share to HLA-DRB1 Chains

Share to HSP70 Heat-Shock Proteins

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Share to Protein Structure, Tertiary

Source

Identifiers

PMID: 12037598
DOI: 10.1007/s00251-002-0444-x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Possible association of non-binding of HSP70 to HLA-DRB1 peptide sequences and protection from rheumatoid arthritis.PMID 12037598Read ↗

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