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  •    Professor
  • Biochemistry
  • Ph.D. 1995, Harvard University

Contact information

Tel: (office) +82-42-350-2839, (lab) +82-42-350-2879, 5839
Location: (office) Room 603 (Bldg. E6-6), (lab) Room 618, 619 (Bldg. E6-6)
Fax: +82-42-350-2810


Ph.D. Department of Biological Chemistry and Molecular Pharmacology, Harvard University (1990.9-1995.10)
M.S. Department of Chemistry, Seoul National University (1987.3-1989.2)
B.S. Department of Chemistry, Seoul National University (1983.3-1987.2)


Sep. 2008- Present Professor, KAIST
Mar. 2004- Aug. 2008 Associate professor, KAIST
Feb. 2001- Feb. 2004 Assistant professor, KAIST
Jan. 2000 - Feb. 2001 Assistant professor, University of Maryland at Baltimore County
Jan. 1996 - Jan. 2000 Postdoctoral fellow, Memorial Sloan Kettering Cancer Center


Jun.27. 2004 FEBS Letters Young Scientist Award
Nov. 30. 2007 Yea`s Scientist (Korean Science Reporters Association)
Jan. 02. 2008 Year`s KAIST Award (KAIST)
Apr. 01.2008 Scientist of Month (KOSEF)
Apr. 26, 2008 Dupont Science and Technology Award (Dupont Korea)
Nov. 19, 2008 ShimKye Science Award (Pohang Accelerator Lab)
Dec. 05, 2008 2007 Top 100 National Research & Development Award


Brief Introduction

The ligand binding and activation mechanisms of signaling receptors will be studied using the novel "Hybrid Protein Technique". The Hybrid Protein Technique can be used for structural studies of other "difficult" proteins such as transcription complexes, replication machineries and eukaryotic ribosomes, etc.
Structural information about signaling receptors will have a profound impact on the pharmaceutical industry because signaling receptors are targeted by the majority of antibody/protein drugs and many of the chemical drugs under development.

Research topics

Transmembrane signaling receptors mediate complex communication processes between cells and outside environments. They are important not only in basic science but also in pharmaceutical industry because they are targeted by almost all protein therapeutics.
The activation mechanisms of signaling receptors are one of the major unsolved problems in receptor biology. This is mainly because structural studies of transmembrane receptors are limited to separated domains and consequently, structural changes induced by the binding of ligands have only been partially characterized.
During the first year of research, we developed techniques necessary for structure prediction of LRR family proteins, developing large scale hybrid libraries and generation of antibodies useful for hybrid crystallization. Using these techniques, we determined the first crystal structure of the TLR4-MD-2-LPS complex. The manuscript is accepted for publication in Nature.

Representative publications

The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex.
Park BS, Song DH, Kim HM, Choi BS, Lee H, Lee JO.
Nature 2009, 458(7242),1191-5.

Structures of the toll-like receptor family and its ligand complexes.
Jin MS, Lee JO.
Immunity 2008, 29(2), 182-91.

Structures of TLR-ligand complexes.
Jin MS, Lee JO.
Curr Opin Immunol. 2008, 20(4), 414-9.

Application of hybrid LRR technique to protein crystallization
Jin MS, Lee JO.
BMB Rep. 2008, 41(5), 353-7.

Regulation of CD40 reconstitution into a liposome using different ratios
of solubilized LDAO to lipids.
Lee KE, Kim HM, Lee JO, Jeon H, Han SS.
Colloids Surf B Biointerfaces. 2008, 62(1), 51-7.

Crystal structure of the TLR1-TLR2 heterodimer induced by
binding of a tri-acylated lipopeptide.
Jin MS, Kim SE, Heo JY, Lee ME, Kim HM, Paik SG, Lee H, Lee JO.
Cell 2007, 130(6), 1071-82.

Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran.
Kim HM, Park BS, Kim JI, Kim SE, Lee J, Oh SC,
Enkhbayar P, Matsushima N, Lee H, Yoo OJ, Lee JO.
Cell 2007, 130(5), 906-17.