1HDM
HISTOCOMPATIBILITY ANTIGEN HLA-DM
Summary for 1HDM
Entry DOI | 10.2210/pdb1hdm/pdb |
Descriptor | PROTEIN (CLASS II HISTOCOMPATIBILITY ANTIGEN, M ALPHA CHAIN), PROTEIN (CLASS II HISTOCOMPATIBILITY ANTIGEN, M BETA CHAIN) (2 entities in total) |
Functional Keywords | histocompatibility protein, immune system |
Biological source | Homo sapiens (human) More |
Cellular location | Late endosome membrane; Single-pass type I membrane protein: P28067 P28068 |
Total number of polymer chains | 2 |
Total formula weight | 44464.08 |
Authors | Wiley, D.C.,Mosyak, L. (deposition date: 1998-09-09, release date: 1999-09-10, Last modification date: 2024-11-20) |
Primary citation | Mosyak, L.,Zaller, D.M.,Wiley, D.C. The structure of HLA-DM, the peptide exchange catalyst that loads antigen onto class II MHC molecules during antigen presentation. Immunity, 9:377-383, 1998 Cited by PubMed Abstract: The three-dimensional structure of the soluble ecto-domain of HLA-DM has been determined to 2.5 A resolution by X-ray crystallography. HLA-DM has both peptide exchange activity and acts as a chaperone to peptide-free class II MHC molecules. As predicted, the structure is similar to that of classical class II MHC molecules except that the peptide-binding site is altered to an almost fully closed groove. An unusual cavity is found at the center of the region that binds peptides in class II MHC molecules, and a tryptophanrich lateral surface is identified that is a candidate both for binding to HLA-DR, to effect catalysis, and to HLA-DO, an inhibitor. PubMed: 9768757DOI: 10.1016/S1074-7613(00)80620-2 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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