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Background:
| 1989: |
B. S. Department of Chemistry, Seoul National
University, Korea |
| 1991: |
M. S. Department of Chemistry (Biochemistry),
Seoul National University, Korea |
| 1994: |
Ph.D. Department of Chemistry (Biochemistry),
Seoul National University, Korea |
| 1994 - 1998: |
Post-doctoral fellow, Department of Chemistry,
University of California, USA |
| 1998 - 2000: |
Assistant Professor, Plant Molecular Biology and
Biotechnology Research Center, Gyeongsang National University,
Korea |
| 2000 – Present: |
Assistant Professor/Associate Professor, Department
of Molecular Cell Biology, Sungkyunkwan University School of
Medicine, Korea |
Research:
Our ongoing research projects focus on various macromolecules involved in
protein kinesis, cell-cell communication, microbial pathogenesis and Z-DNA biology. These
issues have been received extensive attention as the major questions
of current biology. In addition to the major research areas, we
have established collaborative relationship with some of leading
research groups around the world. Eventually, we aim to apply the structure-functional understanding of these macromolecules
to the structure-based drug development and nanobiotechnology.
1. Protein kinesis
Protein quality control is essential for cell viability by maintaining
the proper function of proteins as well as degrading aggregates
of denatured proteins. Quality control is mediated by molecular
chaperones, convertases and many proteases which act to control
the folding, activation and degradation of proteins in the cell.
Currently we are working on proteases, small heat shock proteins
to understand the molecular mechanism of their functional regulation.
In addition, ubiquitin regulated proteolysis or protein modification of
ubiquitin-like protein is the research topic of our group.
2. Cell-cell communication
Transmission of the environmental signals to inside of the cell
regulates various cellular responses such as cell growth and division.
We are focusing on the structural analyses of the ligand-receptor
interaction which occurs on the plasma membrane as an initial step
of various cellular responses.
3. Microbial pathogenesis
The pathogenesis
of the infectious disease caused by bacteria and virus are being
studied in strcutural aspects. Current projects deal with the quorum
sensing and type III and IV secretion systems in bacteria. In addition, structural proteomics
study of Helicobacter pylori is on the progress. Structural
analyses of some selected proteins in H. pylori will give the clues
to understand the structural basis of this infectious diseases and
be the starting point for structure-based development of drug candidates.
4. Z-DNA biology
Left-handed Z-DNA is a higher energy form of the double helix,
stabilized by negative supercoiling generated by transcription or unwrapping nucleosomes.
Z-DNA is also stabilized by specific protein binding; Z-DNA binding proteins.
It is revealed that Z-DNA or Z-DNA binding proteins has a critical roles in transcription, chromatin remodeling
and viral infection. We are currently working on structural and functional identification of various Z-DNA binding proteins
and their roles in the cells.
Publications (selected):
- Crystal Structure of a B-DNA-Z-DNA junction Reveals Two Extruded Bases.
Ha SC, Lowenhaupt K, Rich A, Kim YG, Kim KK (2005). Nature 437, 1183-1186.
- A poxvirus protein forms a complex with left-handed Z-DNA: crystal structure of a Yatapoxvirus Za bound to DNA. Ha SC, Lokanath NK, Quyen DV, Wu CA, Lowenhaupt K, Rich A, Kim YG, Kim KK. (2004). Proc. Natl. Acad. Aci. USA 101, 14367-14372.
- Crystal Structure of Osmotin, a Plant Antifungal Protein. Min K, Ha SC, Hasegawa PM, Bressan RA, Yun D-J, Kim KK. (2004) Proteins: Structure Function and Genetics 54, 170 - 173.
- Crystal structure of ClpX molecular chaperone from Helicobacter Pylori. Kim DY, Kim KK. (2003). J Biol Chem. 278, 50664-50670.
- Activation mechanism of HSP16.5 from Methanococcus jannaschii. Kim DR, Lee I, Ha SC, Kim KK. (2003). Biochem Biophys Res Commun. 307, 991-998.
- Crystal structure of the protease domain of a heat-shock protein
HtrA from Thermotoga maritime. Kim DY, Kim DR, Ha SC, Lokanath
NK, Lee CJ, Hwang HY, Kim KK. (2003). J Biol Chem 278, 6543-6551.
- Dynamic and clustering model of bacterial chemotaxis receptors:
Structural basis for signaling and high sensitivity. Kim S-H,
Wang W, Kim KK. (2002). Proc. Natl. Acad. Aci. USA
99, 11611-11615.
- Crystal Structure of the Ribosome Recycling Factor from Escherichia
coli. Kim KK, Min S, Suh SW. (2000). EMBO J. 19,
2362-2370.
- Four Helical-Bundle Structure of the Cytoplasmic Domain of a
Serine Chemotaxis Receptor. Kim KK, Yokota H, Kim
S-H (1999). Nature 400, 787-792.
- Crystal Structure of Eukaryotic Translation Initiation Factor
5A from Methanococcus janaschii at 1.8 A Resolution. Kim KK,
Hung LW, Yokota H, Kim R, Kim S-H. (1998). Proc.
Natl. Acad. Aci. USA 95, 10419-10424.
- Crystal Structure of a Small Heat-Shock Protein. Kim KK,
Kim R, Kim S.-H. (1998). Nature 394, 595-599.
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