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Professor Jie-Oh Lee of the Department of Chemistry of KAIST
Professor Jie-Oh Lee of the Department of Chemistry of KAIST was selected as the "KAIST Man of the Year."
Lee was cited for his successful identifying of the three-dimensional structure of protein that causes sepsis. His research is expected to contribute greatly to the development of medicines for immune system treatment.
The prize was given by KAIST President Suh Nam Pyo at the New Year"s ceremony on Jan. 2, 2008 at the KAIST auditorium.
Professor Lee published a series of research papers in Science, one of the world"s most prestigious scientific journals. Most recently, Lee was awarded the "Scientist of the Year" prize by the Korean Science Reporters Association.
2008.01.02 View 13404 -
Professor Jie-Oh Lee awarded 'Scientist of the Year'
Professor Jie-Oh Lee of the Department of Chemistry was awarded the ‘Scientist of the Year’ prize for identifying the three-dimensional structure of protein that causes sepsis, and it was announced by the Korean Science Reporters Association (KOSRA) on November 26th.“Humans have about 30,000 different kinds of proteins, and they all have different structures, just like our faces,” said Professor Lee. “It is extremely helpful to know the three-dimensional shape of proteins when you are trying to understand what their functions in an organism are and trying to develop medicine for them.”
When looking for the three-dimensional structure, protein must first be crystallized and radiated with x-ray, so that reflected x-ray can be interpreted. The three-dimensional structure of sepsis immunity proteins TLR1-TLR2 and TLR4-MD2 could not be found until now because they would not even crystallize.
“I began to doubt if it was even possible to crystallize them because we went through so many failures,” reflected Professor Lee.
In August of last year, after about three years of research, the team finally came up with a new idea. The team decided to ‘stick’ the sepsis immunity protein to protein that easily crystallizes. If the combined structure of sepsis immunity protein and the known protein could be identified, the structure of sepsis immunity protein would be a combined structure subtracted by the known structure.
The three-dimensional structure was obtained with x-ray radiation from combined protein crystal. The combined protein was derived from an insect cell with altered DNA.
“This method seems very simple but no one ever tried it or no one ever succeeded in it,” said Professor Lee.
The result was a horseshoe shaped protein structure. The research team also expects the new protein-combining technology to contribute to the development of a new immune system treatment medicine.
The prize-awarding ceremony was held on November 26th in an event hosted by the Korean Hospital Association.
Also, Professor Ryong Ryoo of the Department of Chemistry was selected as the National Scientist last month.By KAIST Herald on November, 2007
2007.12.21 View 13025 -
Professor Eunjoon Kim's team finds synapse-forming protein
Professor Eunjoon Kim’s team finds synapse-forming protein
- discover a new protein ‘NGL’ that promotes the formation of neuronal synapses
- can presume the cause of various brain disorders including schizophrenia
- will be published at Nature Neuroscience Vol. 9 in September
A new protein that promotes the formation of synapses in human brains was discovered by a Korean research team.
The team led by Eunjoon Kim, Professor of Department of Biological Sciences and Head of Creative Research Group of Synapse Formation), announced that it had discovered a new fact that NGL protein promotes the formation of neuronal synapses and this fact would be published in Nature Neuroscience Vol. 9 on September 18.
Professor Kim’s team discovered that a membrane protein named ‘NGL’ located at post synapse links with other membrane protein named netrin-G in pre synapse, acting as crosslink, and promotes the formation of a new synapse.
‘NGL’ is the second protein found to crosslink synapse, following neuoroligin. With the discovery of this new protein, the principle of synapse formation and the causes of various brain disorders can be presumed.
In the human brain, about more than 100 billion neuron cells and about 10,000 synapses compose neural circuit. A synapse is the place where innervation occurs between neuron cells. The formation of synapse induces the formation of neural circuit, and neural circuit is deeply related with various brain disorders as well as normal development of brains or brain functions.
“As netrin-G linked with NGL is related with schizonphrenia and neuoroligin and synapse crosslinking protein having a similar function with NGL is deeply related with mental retardation and autism, I think NGL is related with various brain disorders including schizophrenia.”
<Explanation of attached photos>
■ Photo1: Experiment for confirming NGL’s ability to form synapse No. 1
Mix ordinary cell (green) revealing NGL at its surface and neuron cell. Axon grows toward NGL (ordinary cell) located in the middle of ten o’clock direction and meets NGL, where NGL induces the formation of pre synapse (red) in the contacting axon.
Whether pre synapse has been formed can be told by the fluorescent dying (red) of pre synapse protein named Synapsin.
- Figure a-b: formation of synapse by NGL
- Figure c-d: transformed NGL losing synapse forming ability cannot form synapse
■ Photo 2: Experiment for confirming NGL’s ability to form synapse No. 2
When beads coated with NGL are scattered on neuron cell, the beads contact with the axon of the neuron cell (the beads are clearly visible at the phase differentiation image in the middle panel). At this time, NGL induces the formation of pre synapse (red) in the axon. Whether pre synapse has been formed can be told by the fluorescent dying (red) of pre synapse protein named SynPhy (panel a) or VGlut1 (panel b).
2006.09.21 View 14734