Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1 View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1993-07

AUTHORS

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

ABSTRACT

The three-dimensional structure of the class II histocompatibility glycoprotein HLA-DR1 from human B-cell membranes has been determined by X-ray crystallography and is similar to that of class I HLA. Peptides are bound in an extended conformation that projects from both ends of an 'open-ended' antigen-binding groove. A prominent non-polar pocket into which an 'anchoring' peptide side chain fits is near one end of the binding groove. A dimer of the class II alpha beta heterodimers is seen in the crystal forms of HLA-DR1, suggesting class II HLA dimerization as a mechanism for initiating the cytoplasmic signalling events in T-cell activation. More... »

PAGES

33-39

References to SciGraph publications

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  • Journal

    TITLE

    Nature

    ISSUE

    6432

    VOLUME

    364

    Author Affiliations

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/364033a0

    DOI

    http://dx.doi.org/10.1038/364033a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1023186100

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/8316295


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