Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1994-03

AUTHORS

L J Stern, J H Brown, T S Jardetzky, J C Gorga, R G Urban, J L Strominger, D C Wiley

ABSTRACT

An influenza virus peptide binds to HLA-DR1 in an extended conformation with a pronounced twist. Thirty-five per cent of the peptide surface is accessible to solvent and potentially available for interaction with the antigen receptor on T cells. Pockets in the peptide-binding site accommodate five of the thirteen side chains of the bound peptide, and explain the peptide specificity of HLA-DR1. Twelve hydrogen bonds between conserved HLA-DR1 residues and the main chain of the peptide provide a universal mode of peptide binding, distinct from the strategy used by class I histocompatibility proteins. More... »

PAGES

215-221

Journal

TITLE

Nature

ISSUE

6468

VOLUME

368

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/368215a0

DOI

http://dx.doi.org/10.1038/368215a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1000873113

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8145819


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