3h9z
From Proteopedia
Crystal structure of the IgE-Fc3-4 domains
Structural highlights
FunctionEvolutionary ConservationCheck, 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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