Crystal structure of mouse H2-M

Daved H. Fremont, Frances Crawford, Philippa Marrack, Wayne A. Hendrickson, John Kappler

Research output: Contribution to journalArticlepeer-review

83 Scopus citations

Abstract

H2-M (HLA-DM in humans) resides in an acidic endosomal compartment, where it facilitates the loading of antigenic peptides into the peptide- binding groove of class II MHC. The crystal structure of a soluble form of H2-M has been solved to 3.1 Å, resolution, revealing a heterodimer with structural similarities to the MHC family of proteins. In contrast to its antigen-presenting cousins, the membrane distal α helices of H2-M pack closely together, occluding most of the binding groove except for a single large pocket near the center. The structure of H2-M has several unique features that may play a role in its function as a molecular chaperone and peptide exchange factor.

Original languageEnglish
Pages (from-to)385-393
Number of pages9
JournalImmunity
Volume9
Issue number3
DOIs
StatePublished - Sep 1998

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