3h9y
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Crystal structure of the IgE-Fc3-4 domains
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Structural highlights
FunctionEvolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe structure of immunoglobulin E (IgE)-Fc(3-4) has been solved in three new crystal forms, providing 13 snapshots of the Fc conformation and revealing a diverse range of open-closed motions among subunit chains and dimers. A more detailed analysis of the open-to-closed motion of IgE-Fc(3-4) was possible with so many structures, and the new structures allow a more thorough examination of the flexibility of IgE-Fc and its implications for receptor binding. The existence of a hydrophobic pocket at the elbow region of the Fc appears to be conformation dependent and suggests a means of regulating the IgE-Fc conformation (and potentially receptor binding) with small molecules. Conformational flexibility in immunoglobulin E-Fc 3-4 revealed in multiple crystal forms.,Wurzburg BA, Jardetzky TS J Mol Biol. 2009 Oct 16;393(1):176-90. Epub 2009 Aug 13. PMID:19682998[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 06:16, 27 November 2024.