Membrane receptors and channels represent the gateway through which the cell senses and responds to its environment. Most physiologically important processes are initiated by the interaction of cell-surface receptors/channels with extracellular mediators. This recognition event is communicated across the membrane, resulting in activation of intracellular signal transduction cascades. We ask how information is transmitted across the cell membrane at the molecular level.

It is easy to agree that "Seeing is believing". The roots of our research are in the power of x-ray crystallography and cryo-EM to reveal the structures of biomolecules at atomic level, leading to insights in the physical basis of protein-protein interactions. The core approach is complemented by studies in solution or on membranes by hydrodynamics, small angle x-ray scattering, fluorescence imaging, and various biophysical tools. The structural, biochemical, and biophysical experiments lead to new hypotheses about biological function and mechanism. We also try to demonstrate our new hypotheses in cells using various cell biological tools.

Structures of drug target proteins can also be used to discover new lead compounds by structure-based drug discovery (SBDD) method. We are interested in various drug target proteins to treat various diseases including cancer.

• Ph.D. Chemistry, Seoul National University, Korea, 2007
• M.S. Chemistry, Seoul National University, Korea, 2002
• B.S. Food Science and Biotechnology, Seoul National University, Korea, 2000

• Assistant Professor, Department of Bio & Nano Chemistry, Kookmin University, 2010-2014
• Postdoctoral Fellow, NIDDK, National Institutes of Health, USA, 2007-2010
• Postdoctoral Researcher, The Research Institute of Basic Sciences, Seoul National University, 2007-2007

1. Min, K.; An, D. R.; Yoon, H. J.; Rana, N.; Park, J. S.; Kim, J.; Lee, M.; Hesek, D.; Ryu, S.; Kim, B. M.; Mobashery, S.; Suh, S. W.; Lee, H. H. Peptidoglycan reshaping by a noncanonical peptidase for helical cell shape in Campylobacter jejuni. Nat. Commun. 2020, 11 (1), 458.
2. Kim, M.; Kim, H. J.; Son, S. H.; Yoon, H. –J.; Lim, Y.; Lee, J. W.; Seok, Y. –J.; Jin, K. S.; Yu, Y. G.; Kim, S. K.; Ryu, S.; Lee, H. H. Non-canonical DNA binding mode of repressor and its disassembly by anitrepressor. Proc. Natl. Acad. Sci. USA 2016, 113 (18), E2480-2488.
3. Lee, W. K.; Son, S. H.; Jin, B. S.; Na, J. H.; Kim, S. Y.; Kim, E. K.; Yu, Y. G.; Lee, H. H. Structural and functional insights into the regulation mechanism of CK2 by IP6 and the intrinsically disordered protein Nopp140. Proc. Natl. Acad. Sci. USA 2016, 110 (48), 19360-19365.
4. Kim, H. J.; Yoon, J.; Matsuura, A.; Na, J. H.; Lee, W. K.; Kim, H.; Choi, J. W.; Park, J. E.; Park, S. J.; Kim, K.; Chang, R.; Lee, B. I.; Yu, Y. G.; Shin, Y. K.; Jeong, C.; Rhee, K.; Lee, H. H. Structural and biochemical insights into the role of TEX14 in forming the stable intercellular bridges of germ cells. Proc. Natl. Acad. Sci. USA 2015, 112 (40), 12372-12377.
5. Lee, H. H.; Elia, N.; Ghirlando, R.; Lippincott-Schwartz, J.; Hurley, J. H. Midbody targeting of the ESCRT machinery by a noncanonical coiled coil in CEP55. Science 2008, 322 (5901), 576-580.
6. Lee, H. H.; Kim, Y. S.; Kim, K. H.; Heo, I.; Kim, S. K.; Kim, O.; Kim, H. K.; Yoon, J. Y.; Kim, H. S.; Kim, D. J.; Lee, S. J.; Yoon, H. J.; Kim, S. J.; Lee, B. G.; Song, H. G.; Kim, V. N.; Park, C. M.; Suh, S. W. Structural and functional insight into Dom34, a key component of No-Go mRNA decay. Mol. Cell 2007, 27 (6), 938-950.