Crystal structure of the human high-affinity IgE receptor

Article Abstract:

The binding of immunoglobulin E (IgE) to its high-affinity receptor is necessary to trigger allergic reactions to several environmental compounds. The X-ray crystal structure of the antibody-binding domains of the human IgE receptor at 2.4 angstrom resolution is solved. The receptor is developed from two truncated Ig domains that form a bent two-domain structure that is unlike other coupled Ig domain structures. The crystal structure of the IgE receptor provides insights into the formulation of allergy treatment.

Allergy, Fc receptors

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The emerging field of receptor-mediated inhibitory signaling: SHP or SHIP?

Article Abstract:

The research and development of model systems for receptor-mediated inhibitory signaling have improved data on the molecular mechanisms of signal transduction. Receptors such as FcgammaRIIb1, KIR and CTLA-4 mediate the inhibitory activity of SH2-containing tyrosine phosphatase-1 (SHP-1) and SH2-containing inositol-5prime-phosphatase (SHIP). Furthermore, tyrosine phosphorylation-mediated signals are blocked by the SHP-1 and SHP-2 proteins while SHIP proteins mediate tyrosine phosphorylation.

Cellular signal transduction, Physiological regulation, Biological control systems, Cell receptors, Tyrosine in the body, Tyrosine

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The Fc-epsilon-RI-beta subunit functions as an amplifier of Fc-epsilon-RI-gamma-mediated cell activation signals

Article Abstract:

The high affinity immunoglobulin E receptor (Fc-epsilon-RI) gamma dimer acts as an activator of Syk tyrosine kinase while the beta subunit acts as an amplifier of the gamma subunit. A comparison of the signaling characteristics of different wild-type and mutant alpha-gamma-2 and alpha-beta-gamma-2 dimers of Fc-epsilon-RI determines the role of the beta subunit. Polymorphisms in the beta subunit result in the formation of allergic phenotypes.

Mutation (Biology), Mutation, Protein tyrosine kinase, Protein-tyrosine kinase, Genetic polymorphisms

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