What We Do

Our research group is interested in the structural characterization of protein complex involving cell-cell communications such as cell-cell interactions and receptor-ligand interactions, and their subsequent signaling pathways. These structural information of protein complex can unveil their underlying molecular mechanism such as how proteins interact with each other, how they undergo conformational changes upon by their interactions, and how they perform subsequent signalings. For this, we use not only the traditional molecular biology/biochemistry but also two biophysical cutting edge techniques – X-ray crystallography and Single particle EM. We facilitate protein expression and purification in a wide range of systems, including bacteria, insect cells and mammalian cells. In parallel, based on the structure of disease-related protein complex, we design new therapeutic hybrid proteins and further develop them as potential biologics. 

 

Research Interests

Molecular NeuroScience

 

  • Structure of Synapse Protein

  • Cellular Signaling for Synaptogenesis

 

Structure of Leucine-Rich Repeat (LRR) containing Protein

 

  • Pattern Recognition Receptor in Innate Immunity - TLR Family

  • Hagfish Antibody - Variable Lymphocyte Receptor (VLR)

  • Synaptic Adhesion Molecule - Slitrk Family

 

Protein Engineering using Structural Information of Receptor/Lignad Complex 

 

  • Anti-Angiogenic Protein Therapeutics for Treatments of Cancer and Age-related Macular Degeneration (AMD)

  • Pro-Angiogenic Protein Therapeutics targeting Angiopoietin/Tie2, Wnt, TGF-beta signalings 

 

LAR-RPTP/Slitrk
LAR-RPTP/Slitrk

Structural basis for LAR-RPTP/Slitrk complex-mediated synaptic adhesion. Nat Commun. 2014 Nov 14; 5:5423. doi: 10.1038/ncomms6423

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Proteasome
Proteasome

Reconfiguration of the proteasomeduring chaperone-mediated assembly. Nature, 2013 May 23; 497(7450):512-6

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TLR4-MD2
TLR4-MD2

Crystal structure of theTLR4-MD-2 complex with bound endotoxin antagonist Eritoran. Cell, 2007 Sep 7; 130(5):906-17

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VLR
VLR

Structural diversity of the hagfish variable lymphocyte receptors. The Journal of Biological Chemistry. 282(9): 6726-32 (2007)

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