PMID: 9188169Jan 1, 1997Paper

Automated hydrodynamic modelling of a complex between a human IgE fragment (Fc epsilon 3-4) and the IgE high affinity receptor Fc epsilon RI alpha-chain

European Biophysics Journal : EBJ
A J Beavil, R L Beavil

Abstract

The binding of IgE to its high affinity receptor Fc epsilon RI plays an important role in the allergic response. The interaction between soluble Fc epsilon RI alpha-chain (sFc epsilon RI alpha) and Fc epsilon 3-4, a fragment of IgE consisting of the C epsilon 3 and C epsilon 4 heavy chain constant domains, has been studied using analytical ultracentrifugation (Keown et al. this volume). Here we describe the development of a simple automated hydrodynamic modelling technique and its application to this interaction. This procedure utilises sphere models of the two molecules and performs an automated systematic translational search of sFc epsilon RI alpha relative to Fc epsilon 3-4. The result of this is the generation of 40,359 individual models of how the receptor can be placed relative to Fc epsilon 3-4. These are then assessed for consistency by comparing the sedimentation coefficients generated for the models to the experimentally determined sedimentation coefficients, and are displayed graphically to show allowed and disallowed complexes. From this analysis, it is clear that the complex between sFc epsilon RI alpha and Fc epsilon 3-4 is compact, with the most elongated models being excluded. In addition, sFc epsilon RI alpha ...Continue Reading

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