Ontology highlight
ABSTRACT:
SUBMITTER: Mizushima T
PROVIDER: S-EPMC3258418 | biostudies-literature | 2011 Nov
REPOSITORIES: biostudies-literature
Mizushima Tsunehiro T Yagi Hirokazu H Takemoto Emi E Shibata-Koyama Mami M Isoda Yuya Y Iida Shigeru S Masuda Kazuhiro K Satoh Mitsuo M Kato Koichi K
Genes to cells : devoted to molecular & cellular mechanisms 20111101 11
Removal of the fucose residue from the N-glycans of the Fc portion of immunoglobulin G (IgG) results in a dramatic enhancement of antibody-dependent cellular cytotoxicity (ADCC) through improved affinity for Fcγ receptor IIIa (FcγRIIIa). Here, we present the 2.2-Å structure of the complex formed between nonfucosylated IgG1-Fc and a soluble form of FcγRIIIa (sFcγRIIIa) with two N-glycosylation sites. The crystal structure shows that one of the two N-glycans of sFcγRIIIa mediates the interaction w ...[more]