By Jeffrey V. Ravetch (auth.), Max D. Cooper M.D., Toshiyuki Takai Ph.D., Jeffrey V. Ravetch M.D., Ph.D. (eds.)
A amazing spectrum of novel immunoreceptors sharing similar immunoglobulin-like domain names and signaling power has been pointed out in recent times. those receptors have attracted frequent curiosity simply because they resemble the TCR, BCR, and FcR complexes of their skill to function activating or inhibitory receptors at the cells that endure them. in addition, they're good situated to impact either innate and adaptive immunity. the whole variety of ligands for those new receptor households continues to be no longer identified, and figuring out in their physiological roles is way from whole. This quantity is the 1st try and summarize and spotlight all recognized points of immunoglobulin-like receptors, supplying a topical assessment of the jobs and attribute good points of the immunoglobulin-like receptors and similar molecules within the immune approach. Researchers in immunology, molecular biology, cellphone biology, scientific drugs, and pharmacology will locate this publication invaluable.
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Extra info for Activating and Inhibitory Immunoglobulin-like Receptors
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Additionally the structures of the activating FcRs , FcyRIla (Max well et al. 1999), FcyRIII (Sondermann et al. 2(00) and Fcskln (Garman et al. 1998), have been determined. The Ig domains in these receptors have a characteristic and unique structure, intermediate between the I-set and C2-set Ig folds (Fig. Ib). Although sequence similarity among these Ig-like receptors is not high, this structural similarity suggests they have the same common ancestor receptor. The recently solved structures of the complexes KIR2DL2/HLA-Cw3 (Boyington et al.
Binding to IgG or Fe was analysed by SPR. The affinity of sFcyRs binding to immobilized Fe was measured by equilibrium binding analysis. 5IlM) with very fast dissociation rates (Table 2) (Maenaka et al. unpublished) . We estimated the enthalpy change (~H) which accompanies FcyRs binding to Fe by van't Hoff analysis, which involves measuring the dependence of affinity on temperature. For FcyRIIa and Ilb, at 25°C favourable enthalpic and entropic changes contribute to the binding energy . In contrast FcyRIII binding to IgG or Fe was characterised by large unfavourable entropic changes.