Abstract
Background: CXCL4L1 is a highly potent anti-angiogenic and anti-tumor chemokine, and its structural information is unknown. Results: CXCL4L1 x-ray structure is determined, and it reveals a previously unrecognized chemokine structure adopting a novel C-terminal helix conformation. Conclusion: The alternative helix conformation enhances the anti-angiogenic activity of CXCL4L1 by reducing the glycosaminoglycan binding ability. Significance: Chemokine C-terminal helix orientation is critical in regulating their functions. Copyright © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
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CITATION STYLE
Kuo, J. H., Chen, Y. P., Liu, J. S., Dubrac, A., Quemener, C., Prats, H., … Sue, S. C. (2013). Alternative C-terminal helix orientation alters chemokine function: Structure of the anti-angiogenic chemokine, CXCL4L1. Journal of Biological Chemistry, 288(19), 13522–13533. https://doi.org/10.1074/jbc.M113.455329
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