1K8I
CRYSTAL STRUCTURE OF MOUSE H2-DM
Summary for 1K8I
Entry DOI | 10.2210/pdb1k8i/pdb |
Descriptor | MHC class II H2-M alpha chain, MHC class II H2-M beta 2 chain, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
Functional Keywords | mhc, immune system |
Biological source | Mus musculus (house mouse) More |
Total number of polymer chains | 2 |
Total formula weight | 43239.24 |
Authors | Fremont, D.H.,Crawford, F.,Marrack, P.,Hendrickson, W.,Kappler, J. (deposition date: 2001-10-24, release date: 2001-12-05, Last modification date: 2024-11-13) |
Primary citation | Fremont, D.H.,Crawford, F.,Marrack, P.,Hendrickson, W.A.,Kappler, J. Crystal structure of mouse H2-M. Immunity, 9:385-393, 1998 Cited by PubMed 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 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. PubMed: 9768758DOI: 10.1016/S1074-7613(00)80621-4 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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