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Structural Biology & Drug Discovery / Professor Ho Sup Yoon's Lab

Apoptosis; Molecular chaperones in cancer, malaria, and neurodegenerative diseases; Peptidylprolyl cis-trans isomerases; Nuclear Receptors; NMR; Structure-based drug design.

Understanding molecular basis of proteins is a key to delineate their biological functions in cellular pathways and ultimately provides insights into therapeutic strategies. We study the underlying molecular mechanisms of key regulatory proteins, characteristics of protein-protein and protein-ligand interactions by employing cross-disciplinary approaches. Over the years, our multidisciplinary research programmes enabled us to study molecular mechanisms of several key molecules such as phospholipid-interacting proteins, Bcl-2 family proteins, FK506 binding proteins, Kinases, Nuclear Receptors, and subsequently aided in developing their cognate ligands with therapeutic potential. The resulting outcomes provided us leverage to focus on translational biomedical research, in particular clinically unmet research areas.

Lab Page:​​

Yoon Ho Sup
Research Director, Biomedical Sciences
Professor, School of Biological Sciences

Office: ADM-03-05A/ SBS-02S-96
Sreekanth Rajan
Senior Research Fellow

Rishikesan Sankaranarayanan
Research Fellow

Toh Hui Ting
Research Assistant

Gan Hanjie Jonathan
PhD student


  • Characterization and search for novel extracellular proteases in Bacillus subtilis for industrial use
  • In vitro and in vivo studies of Suprafenacine, a novel microtubule destabilizing anti-cancer drug
  • Nucleic acid recognition by FK506-binding protein 25 (FKBP25), a nuclear immunophilin
  • Regulation of vaccinia-related kinase 1 (VRK1) by mH2A1.1, a histone H2A variant
  • Seeking Selective and Sensitive Ligands for Hemagglutinin of H7N9 Influenza Virus: A Potential Sugarcode- based Diagnostic
  • Selective inhibitors of VRK1, a mitotic kinase
  • Toward development of a new class of anti-malaria drug : molecular characterization and three-dimensional structure determination of plasmodium falciparum FK506-binding protein 35 (PfFKPB35)
  • Understanding Molecular Mechanism of Supradamal, a Novel Adamantanyl-Based Antimalarial Drug
  • Validation of Nurr1 Ligands as Potential PD Therapeutics (Theme 5 - Experimental Therapeutics)

Full list of publications can be found here
  • Beldar S, Manimekalai MSS, Cho NJ, Baek B, Gruber G, Yoon HS (2018) Self-association and conformational variation of NS5A domain 1 of hepatitis C virus. J Gen Virol. 99, 194-208
  • Prakash A, Shin J, Rajan S, Yoon HS (2016) Structural basis of nucleic acid recognition by human FK506-binding protein 25 (FKBP25), a nuclear immunophilin. Nucleic Acids Res. 44, 2909-25
  • Kim CH, Han, BS, Moon J, Kim DJ, Shin J, Rajan S, Toh HT, Sohn M, Kim WG, Han M, Jeong I, Kim KS, Lee EH, TU, Y, Naffin-Olivos JL, Park CH, Ringe D, Yoon HS, Petsko GA, and Kim KS (2015) Agonists for Nurr1 enhance its contrasting dual functions and ameliorate Parkinson-related phenotypes. Proc. Natl. Acad. Sci. USA. 112, 8756-8761.
  • Rajan S, Choi M, Nguyen QT, Ye H, Liu W, Toh HT, Kang CB, Kamariah N, Grüber G, Li C, Huang H, White C, Baek K, and Yoon HS (2015) Structural transition in Bcl-xL and its potential association with mitochondrial calcium ion transport. Sci Rep. 2015 May 29;5:10609. doi: 10.1038/srep10609.
  • He S, Ni D, Ma B, Lee JH, Zhang T, Ghozalli I, Pirooz SD, Zhao Z, Nagakumar B, Li B,Oh S, Lee WH, Takahashi Y, Wang HG, Deretic V, Pepperkok R, Tagaya M, Yoon HS, and Chengyu Liang (2013) PI(3)P-bound UVRAG coordinates Golgi-ER retrograde and Atg9 transport by differential interactions with the ER tether and the Beclin1 complex. Nature Cell Biology 15, 1206-1219.
  • Shin J, Chakraborty G, Bharatham N, Tochio N, Koshiba S, Kigawa T, Kim W, Kim KT, Yoon HS (2011) NMR solution structure of human vaccinia-related kinase 1 (VRK1) reveals the C-terminal tail essential for structural stability and autocatalytic activity. J. Biol. Chem. 286, 22131-22138.
  • Won EY, Jang M, Lee DH, Ryu KS, Bae KH, Park BC, Yoon HS*, and Chi, SW* (2011) Molecular-mimicry-based repositioning of Nutlin-3 to anti-apoptotic Bcl-2 family proteins. J. Am. Chem. Soc. 133, 1244-1247 (*co-corresponding author).
  • Choi BH, Feng L and Yoon HS (2010) FKBP38 Protects Bcl-2 from caspase-dependent degradation. J. Biol. Chem. 285, 9770-9779.
  • Muchmore SW, Sattler M, Liang H, Meadows RP, Harlan JE, Yoon HS, Nettesheim D, Chang BS, Thompson CB, Wong SL, Ng SC, and Fesik SW (1996) X-ray and NMR structure of Bcl-XL, an inhibitor of programmed cell death. Nature 381, 335-341.
  • Yoon HS, Hajduk PT, Petros AM, Olejniczak ET, Meadows RP, and Fesik SW (1994) Solution structure of a Pleckstrin homology (PH) domain. Nature 369, 672-675.
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