Functional interaction of the ankylosing spondylitis-associated endoplasmic reticulum aminopeptidase 1 polymorphism and HLA-B27 in vivo.

@article{GarcaMedel2012FunctionalIO,
  title={Functional interaction of the ankylosing spondylitis-associated endoplasmic reticulum aminopeptidase 1 polymorphism and HLA-B27 in vivo.},
  author={Noel Garc{\'i}a-Medel and Alejandro Sanz-Bravo and Dung Van Nguyen and Bego{\~n}a Galocha and Patricia G{\'o}mez-Molina and Adri{\'a}n Mart{\'i}n-Esteban and Carlos Alvarez-Navarro and Jos{\'e} Antonio L{\'o}pez de Castro},
  journal={Molecular & cellular proteomics : MCP},
  year={2012},
  volume={11 11},
  pages={1416-29}
}
The association of ERAP1 with ankylosing spondylitis (AS)1 among HLA-B27-positive individuals suggests that ERAP1 polymorphism may affect pathogenesis by altering peptide-dependent features of the HLA-B27 molecule. Comparisons of HLA-B*27:04-bound peptidomes from cells expressing different natural variants of ERAP1 revealed significant differences in the size, length, and amount of many ligands, as well as in HLA-B27 stability. Peptide analyses suggested that the mechanism of ERAP1/HLA-B27… CONTINUE READING
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The crystal structure of human endoplasmic reticulum aminopeptidase 2 reveals the atomic basis for distinct roles in antigen processing

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