Conformational flexibility in immunoglobulin E-Fc 3-4 revealed in multiple crystal forms.
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.
Wurzburg
Beth A
BA
Department of Structural Biology, Stanford University, Stanford, CA 94305, USA.
Jardetzky
Theodore S
TS
D018360:Crystallography, X-Ray; D006801:Humans; D007073:Immunoglobulin E / Q000737:chemistry*; D007141:Immunoglobulin Fc Fragments / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D020836:Protein Structure, Quaternary
D007141:Immunoglobulin Fc Fragments; D007073:Immunoglobulin E
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