The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1991-09

AUTHORS

D R Madden, J C Gorga, J L Strominger, D C Wiley

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. More... »

PAGES

321-325

Journal

TITLE

Nature

ISSUE

6342

VOLUME

353

Author Affiliations

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/353321a0

    DOI

    http://dx.doi.org/10.1038/353321a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1049183301

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/1922337


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