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Article

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

Journal of immunology (Baltimore, Md. : 1950) - 15 May 1994

Marshall K W, Liu A F, Canales J, Perahia B, Jorgensen B, Gantzos R D, Aguilar B, Devaux B, Rothbard J B

Abstract excerpt

Analysis of peptide binding to a set of HLA-DR alleles has allowed the proteins to be segregated into functional subsets, depending on the amino acids at positions 57 and 86 of the beta-chain. DR proteins with glycine at 86 beta and aspartic acid at 57 beta bound a simplified peptide with significantly lower IC50 values than alleles that did not have this combination of amino acids. The size of the amino acid at...

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Source

Identifiers

PMID: 8176213

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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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Role of the polymorphic residues in HLA-DR molecules in allele-specific binding of peptide ligands.PMID 8176213Read ↗

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