title: Human antibody-Fc receptor interactions illuminated by crystal structures.
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.
authors.affiliation: Division of Pathology and Neuroscience, University of Dundee Medical School, Ninewells Hospital, Dundee DD1 9SY, UK. j.m.woof@dundee.ac.uk
authors.forename: Jenny M
authors.initials: JM
authors.lastname: Woof
authors.forename: Dennis R
authors.initials: DR
authors.lastname: Burton
mesh_terms: D000906:Antibodies / Q000737:chemistry* / Q000276:immunology*; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011961:Receptors, Fc / Q000737:chemistry* / Q000276:immunology*; D015398:Signal Transduction
chemical_list: D000906:Antibodies; D011961:Receptors, Fc