TY - JOUR
T1 - Crystal structure of mouse H2-M
AU - Fremont, Daved H.
AU - Crawford, Frances
AU - Marrack, Philippa
AU - Hendrickson, Wayne A.
AU - Kappler, John
N1 - Funding Information:
We thank Amy Marrs and Randy Anselment in the National Jewish Biomolecular Resource Facility for performing the N-terminal sequencing of H2-M and oligonucleotide synthesis. We also thank Daphne Norsworthy in the National Jewish DNA Sequencing Lab for sequencing the H2-M constructions. Special thanks to Chris Lima, Chris Nelson, and Kyunghee Choi for fruitful discussions. D. H. F. is the recipient of a Burroughs-Wellcome Fund Career Award in the Biomedical Sciences and is supported in part by the Kilo Diabetes and Vascular Research Foundation. This work was supported in part by United States Public Health Services Grants AI-17134, AI-22295 and AI-18785.
PY - 1998/9
Y1 - 1998/9
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0032167447&partnerID=8YFLogxK
U2 - 10.1016/S1074-7613(00)80621-4
DO - 10.1016/S1074-7613(00)80621-4
M3 - Article
C2 - 9768758
AN - SCOPUS:0032167447
SN - 1074-7613
VL - 9
SP - 385
EP - 393
JO - Immunity
JF - Immunity
IS - 3
ER -