The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation.

Article Details

Citation

Madden DR, Gorga JC, Strominger JL, Wiley DC

The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation.

Nature. 1991 Sep 26;353(6342):321-5.

PubMed ID
1922337 [ View in PubMed
]
Abstract

X-ray crystallography reveals electron density in the antigen-binding site of HLA-B27 that is an interpretable image of nonameric peptides in a largely extended conformation. Clear density exists for the main chain and several side chains and is consistent with the sequence of 11 nonameric self-peptides eluted from HLA-B27. Pockets in the antigen-binding cleft bind four side chains and the amino and carboxyl termini of the peptide.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
HLA class I histocompatibility antigen, B-27 alpha chainP01889Details