Differential effect of polymorphism at HLA-DR1 beta-chain positions 85 and 86 on binding and recognition of DR1-restricted antigenic peptides.

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Article

Differential effect of polymorphism at HLA-DR1 beta-chain positions 85 and 86 on binding and recognition of DR1-restricted antigenic peptides.

Journal of immunology (Baltimore, Md. : 1950) - 1 Mar 1993

Newton-Nash D K, Eckels D D

Abstract excerpt

The valine-glycine dimorphism at position 86 of the DR beta-chain exhibited by most DR alleles has been shown to affect peptide binding. We demonstrate that DR1-restricted antigenic peptides differ in the extent to which binding is affected by amino acid substitution at positions 85 and 86 of the...

Topics

Alleles
Amino Acid Sequence
Binding, Competitive
Epitopes
HLA-DR Antigens
Humans
Lymphocyte Activation
Molecular Sequence Data
Peptide Fragments
Polymorphism, Genetic
Protein Conformation
Structure-Activity Relationship
T-Lymphocytes

Source

Open in PubMed

Identifiers

PMID: 7679697

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7679697-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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