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Updated: Aug 7, 2026

Optimized Negative Staining: a High-throughput Protocol for Examining Small and Asymmetric Protein Structure by Electron Microscopy
Published on: August 15, 2014
Human antibody-Fc receptor interactions illuminated by crystal structures
Jenny M Woof1, Dennis R Burton
1Division of Pathology and Neuroscience, University of Dundee Medical School, Ninewells Hospital, Dundee DD1 9SY, UK. j.m.woof@dundee.ac.uk
Abstract:
Immunoglobulins couple the recognition of invading pathogens with the triggering of potent effector mechanisms for pathogen elimination. Different immunoglobulin classes trigger different effector mechanisms through interaction of immunoglobulin Fc regions with specific Fc receptors (FcRs) on immune cells. Here, we review the structural information that is emerging on three human immunoglobulin classes and their FcRs. New insights are provided, including an understanding of the antibody conformational adjustments that are required to bring effector cell and target cell membranes sufficiently close for efficient killing and signal transduction to occur. The results might also open up new possibilities for the design of therapeutic antibodies.
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