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|3h9y, resolution 2.23Å ()|
|Sites:||, , , , , , , , , , , , , , , and|
|Non-Standard Residues:||, ,|
|Gene:||IGHE (Homo sapiens)|
|Related:||1fp5, 1f6a, 1o0v, 3h9z, 3ha0|
Crystal structure of the IgE-Fc3-4 domains
The 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 Aug 13. PMID:19682998
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Wurzburg BA, Jardetzky TS. Conformational flexibility in immunoglobulin E-Fc 3-4 revealed in multiple crystal forms. J Mol Biol. 2009 Oct 16;393(1):176-90. Epub 2009 Aug 13. PMID:19682998 doi:10.1016/j.jmb.2009.08.012
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