Ontology highlight
ABSTRACT:
SUBMITTER: Oganesyan V
PROVIDER: S-EPMC4631484 | biostudies-literature | 2015 Nov
REPOSITORIES: biostudies-literature
Oganesyan Vaheh V Mazor Yariv Y Yang Chunning C Cook Kimberly E KE Woods Robert M RM Ferguson Andrew A Bowen Michael A MA Martin Tom T Zhu Jie J Wu Herren H Dall'Acqua William F WF
Acta crystallographica. Section D, Biological crystallography 20151031 Pt 11
The three-dimensional structure of a human IgG1 Fc fragment bound to wild-type human FcγRI is reported. The structure of the corresponding complex was solved at a resolution of 2.4 Å using molecular replacement; this is the highest resolution achieved for an unmutated FcγRI molecule. This study highlights the critical structural and functional role played by the second extracellular subdomain of FcγRI. It also explains the long-known major energetic contribution of the Fc `LLGG' motif at positio ...[more]