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Article

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

The Journal of biological chemistry - 10 Dec 2010

Galocha Begoña, López de Castro José A

Abstract excerpt

Molecular polymorphism influences the strong association of HLA-B27 with ankylosing spondylitis through an unknown mechanism. Natural subtypes and site-directed mutants were used to analyze the effect of altering the peptide-binding site of this molecule on its stability, interaction with tapasin, folding, and export. The disease-associated subtypes B*2705, B*2702, and B*2704 showed higher thermostability at 50...

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Source

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Identifiers

PMID: 20889980
DOI: 10.1074/jbc.M110.149906
PMCID: PMC2998085

Provenance

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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Mutational analysis reveals a complex interplay of peptide binding and multiple biological features of HLA-B27.PMID 20889980Read ↗

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