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Article

Modulation of peptide binding by HLA-B27 polymorphism in pockets A and B, and peptide specificity of B*2703.

European journal of immunology - 1 Aug 1995

Villadangos J A, Galocha B, García F, Albar J P, López de Castro J A

Abstract excerpt

The results in this study address three aspects of peptide binding to the disease-associated antigen HLA-B27 and its modulation by polymorphism: the contribution of major anchor residues 2 and 9, the role of pocket B polymorphism in modulating peptide specificity, and the binding properties of B*2703, a subtype not found to be associated with spondyloarthropathy. Synthetic analogs of peptides naturally presented...

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Source

Identifiers

PMID: 7664799
DOI: 10.1002/eji.1830250837

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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.

Related research

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Modulation of peptide binding by HLA-B27 polymorphism in pockets A and B, and peptide specificity of B*2703.PMID 7664799Read ↗

The Peptide Repertoires of HLA-B27 Subtypes Differentially Associated to Spondyloarthropathy (B*2704 and B*2706) Differ by Specific Changes at Three Anchor PositionsSemantic proximity Read ↗

Naturally occurring A pocket polymorphism in HLA-B*2703 increases the dependence on an accessory anchor residue at P1 for optimal binding of nonamer peptides.Semantic proximity Read ↗

The Cys-67 residue of HLA-B27 influences cell surface stability, peptide specificity, and T-cell antigen presentation.Semantic proximity Read ↗

Binding of peptides naturally presented by HLA-B27 to the differentially disease-associated B*2704 and B*2706 subtypes, and to mutants mimicking their polymorphism.Semantic proximity Read ↗

Allele-specific B pocket transplant in class I major histocompatibility complex protein changes requirement for anchor residue at P2 of peptide.Semantic proximity Read ↗

Anchoring pockets in human histocompatibility complex leukocyte antigen (HLA) class I molecules: analysis of the conserved B ("45") pocket of HLA-B27.Semantic proximity Read ↗

Comparison of the P2 specificity pocket in three human histocompatibility antigens: HLA-A*6801, HLA-A*0201, and HLA-B*2705.Semantic proximity Read ↗

Several HLA alleles share overlapping peptide specificities.Semantic proximity Read ↗

Susceptibility to ankylosing spondylitis correlates with the C‐terminal residue of peptides presented by various HLA‐B27 subtypesSemantic proximity Read ↗

Differences in peptide presentation between B27 subtypes: the importance of the P1 side chain in maintaining high affinity peptide binding to B*2703.Semantic proximity Read ↗

Changes in the repertoire of peptides bound to HLA-B27 subtypes and to site-specific mutants inside and outside pocket B.Semantic proximity Read ↗

Mutational analysis reveals a complex interplay of peptide binding and multiple biological features of HLA-B27.Semantic proximity Read ↗

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