Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 393, Issue 1, Pages 176-190Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2009.08.012
Keywords
IgE-Fc; crystal structure; flexibility; hydrophobic pocket
Categories
Funding
- E. I. DuPont de Nemours Co.
- Dow Chemical Company
- U.S. National Science Foundation [DMR-9304725]
- State of Illinois through the Department of Commerce
- Board of Higher Education [IBHE HECA NWU 96]
- U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [W-31109-Eng-38]
- National Institutes of Health [AI18939]
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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. (C) 2009 Elsevier Ltd. All rights reserved.
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