| First Author | Fremont DH | Year | 1998 |
| Journal | Immunity | Volume | 9 |
| Issue | 3 | Pages | 385-93 |
| PubMed ID | 9768758 | Mgi Jnum | J:50220 |
| Mgi Id | MGI:1290041 | Doi | 10.1016/s1074-7613(00)80621-4 |
| Citation | Fremont DH, et al. (1998) Crystal structure of mouse H2-M. Immunity 9(3):385-93 |
| abstractText | 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 A resolution, revealing a heterodimer with structural similarities to the MHC family of proteins. In contrast to its antigen-presenting cousins, the membrane distal alpha 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. |
