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Article

Effect of natural polymorphism at residue 86 of the HLA-DR beta chain on peptide binding.

Journal of immunology (Baltimore, Md. : 1950) - 15 Aug 1991

Busch R, Hill C M, Hayball J D, Lamb J R, Rothbard J B

Abstract excerpt

Class I and class II MHC glycoproteins are highly polymorphic molecules that bind antigenic peptides and present them on cell surfaces for recognition by T lymphocytes. Even though MHC polymorphism has long been known to affect both peptide binding and recognition by the TCR, the role of individual amino acids of MHC proteins in these interactions is poorly understood. To examine the effect of a small number of...

Topics

Alleles
Amino Acid Sequence
B-Lymphocytes
Biotin
HLA-DR Antigens
Hemagglutinin Glycoproteins, Influenza Virus
Hemagglutinins, Viral
Humans
Molecular Sequence Data
Peptides
Polymorphism, Genetic

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PMID: 1869824

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1869824-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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Effect of natural polymorphism at residue 86 of the HLA-DR beta chain on peptide binding.PMID 1869824Read ↗

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

Role of the polymorphic residues in HLA-DR molecules in allele-specific binding of peptide ligands.Semantic proximity Read ↗

Individual effects of the DR11-variable beta-chain residues 67, 71, and 86 upon DR(alpha,beta 1*1101)-restricted, peptide-specific T cell proliferation.Semantic proximity Read ↗

Implication of HLA-DR residues at positions 67, 71, and 86 in interaction between HLA-DR11 and peptide HA306-320.Semantic proximity Read ↗

Polymorphism at beta 85 and not beta 86 of HLA-DR1 is predominantly responsible for restricting the nature of the anchor side chain: implication for concerted effects of class II MHC polymorphism.Semantic proximity Read ↗

Effects of localized HLA class II beta chain polymorphism on binding of antigenic peptide and stimulation of T cells.Semantic proximity Read ↗

Structural basis of specificity and degeneracy of T cell recognition: pluriallelic restriction of T cell responses to a peptide antigen involves both specific and promiscuous interactions between the T cell receptor, peptide, and HLA-DR.Semantic proximity Read ↗

Peptide binding to HLA-DR1: a peptide with most residues substituted to alanine retains MHC binding.Semantic proximity Read ↗

Critical contribution of beta chain residue 57 in peptide binding ability of both HLA-DR and -DQ molecules.Semantic proximity Read ↗

Distant interactions between dimorphisms in HLA-DR4 radically affect recognition of defined peptides by a specific T cell clone.Semantic proximity Read ↗

Critical role for the Val/Gly86 HLA-DR beta dimorphism in autoantigen presentation to human T cells.Semantic proximity Read ↗

The set of naturally processed peptides displayed by DR molecules is tuned by polymorphism of residue 86.Semantic proximity Read ↗

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