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Full-Text Articles in Medicine and Health Sciences
Effects Of Anchor Structure And Glycosylation Of Fcî³ Receptor Iii On Ligand Binding Affinity, Ning Jiang, Wei Chen, Prithiviraj Jothikumar, Jaina M. Patel, Rangaiah Shashidharamurthy, Periasamy Selvaraj, Cheng Zhu
Effects Of Anchor Structure And Glycosylation Of Fcî³ Receptor Iii On Ligand Binding Affinity, Ning Jiang, Wei Chen, Prithiviraj Jothikumar, Jaina M. Patel, Rangaiah Shashidharamurthy, Periasamy Selvaraj, Cheng Zhu
PCOM Scholarly Papers
Isoforms of the Fcγ receptor III (FcγRIII or CD16) are cell surface receptors for the Fc portion of IgG and important regulators of humoral immune responses. Different ligand binding kinetics of FcγRIII isoforms are obtained in three dimensions by surface plasmon resonance and in two dimensions by a micropipette adhesion frequency assay. We show that the anchor structure of CD16 isoforms isolated from the cell membrane affects their binding affinities in a ligand-specific manner. Changing the receptor anchor structure from full to partial to none decreases the ligand binding affinity for human IgG1 (hIgG1) but increases it for murine IgG2a …