3H9Z

Crystal structure of the IgE-Fc3-4 domains

Summary for 3H9Z

• Entry DOI: 10.2210/pdb3h9z/pdb
• Related: 1F6A 1FP5 1O0V 3H9Y 3HA0
• Descriptor: Ig epsilon chain C region, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, AMMONIUM ION, ... (4 entities in total)
• Functional Keywords: immunoglobin, ige, fc, flexibility, hydrophobic pocket, disulfide bond, glycoprotein, immunoglobulin c region, immunoglobulin domain, immune system
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 4
• Total formula weight: 102431.09

Authors

Wurzburg, B.A. (deposition date: 2009-04-30, release date: 2009-09-08, Last modification date: 2024-10-16)

Primary citation

Wurzburg, B.A.,Jardetzky, T.S.
Conformational flexibility in immunoglobulin E-Fc 3-4 revealed in multiple crystal forms.
J.Mol.Biol., 393:176-190, 2009

PubMed Abstract: 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.

PubMed: 19682998
DOI: 10.1016/j.jmb.2009.08.012

Experimental method

X-RAY DIFFRACTION (2.45 Å)