Xiaoling Xu, Ph.D.
Research
Natural alternative forms of human tryptophanyl-tRNA synthetase (TrpRS) have potent anti-angiogenic activity. This activity is blocked until the N-terminal domain (N-domain) is removed, either by alternative splicing to give mini-TrpRS, or by proteolysis, to give the closely similar T2-TrpRS. T2-TrpRS binds to the endothelial cell adherens junction molecule¾vascular endothelial-cadherin (VE-cadherin), and inhibits activation of genes associated with angiogenesis such as Akt and endothelial cell NO synthase. Because it inhibits new blood vessel formation, with no disruption of existing blood vessels, T2-TrpRS has appeal for therapeutic applications, including macular degeneration and oncology. My research is focused on the mechanism of anti-angiogenesis of TrpRS through X-ray crystallography and cell biology.
Publications
Xu X, Lou Z, Ma Y, Rao Z. Crystal structure of the C-terminal cytoplasmic domain of non-structural protein 4 from mouse hepatitis virus A59. 2009. Plos One.
Hui Dong, Zhiyong Lou, Xiaoling Xu, Dan Su, Xiao hong Zhou, Xin Li and Mark Bartlam*. Crystallization and Preliminary Crystallographic Analysis of Recombinant Human Calcyphosine. 2009. Protein and Peptide Letters.16(3):339-41.
Hui Dong, Xin Li, Zhiyohiyong Lou, Xiaoling Xu, Dan Su, Xiaohong zhou, Mark Bartlam* and Zihe Rao. Crystal structure and biochemical characterization of recombinant human calcyphosine delineates a novel EF-hand-containing protein family. 2008. J Mol Biol. 383(3):455-64.
Xu X, Zhai Y, Sun F, Lou Z, Su D, Xu Y, Zhang R, Joachimiak A, Zhang XC, Bartlam M & Rao Z*. New antiviral target revealed by the hexameric structure of mouse hepatitis virus nonstructural protein nsp15. 2006. J Virol, 80(16):7909-7917.
Zhai Y, Sun F, Li X, Pang H, Xu X, Bartlam M, & Rao Z*. Structural insights into coronavirus transcription/replication from the crystal structure of the SARS-CoV hexadecameric Nsp7•Nsp8 super-complex.2005. Nature Structural & Molecular Biology, 12(11): 980-986.
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