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IBS Conferences

Research Centers

 

김호민

Chief InvestigatorKIM Ho Min

  • KIM Ho Min Chief InvestigatorKIM Ho Min

Integrative research on 3D structure and function of proteins for understanding physiology and pathology

Contact Info

Tel. +82-42-878-9400

Fax +82-42-878-9409

Address

IBS Center for Biomolecular and Cellular Structure (Protein Communication Group), 55 Expo-ro, Doryong-dong, Yuseong-gu, Daejeon (34126)

Major Publications

more paper
  • - Reconstruction of LPS transfer cascade reveals structural determinants within LBP, CD14 and TLR4-MD2 for efficient LPS recognition and transfer.
  • - Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran.
  • - Structural Insights into Modulation of Neurexin-Neuroligin Trans-synaptic Adhesion by MDGA1/Neuroligin-2 Complex.
  • - Structural basis for LAR-RPTP/Slitrk complex-mediated synaptic adhesion.
  • - Multi-paratopic VEGF decoy receptor have superior anti-tumor effects through anti-EGFRs and targeted anti-angiogenic activities.
About CI
Protein Communication Group led by Kim Ho Min

CI Kim Ho Min

Professor Kim is the chief investigator of the Protein Communication Group in the PRC Center for Biomolecular and Cellular Structure, established in December 2018. He received his Ph.D. from the Department of Biological Science in the Korea Advanced Institute of Science & Technology (KAIST) in the field of structural biology, specializing in X-ray crystallography. He completed three postdoctoral fellowships, with the first two at KAIST and then the final at the University of California, San Francisco where conducted advanced training with Cryo-EM (2007~2011). He then to KAIST where he started as an assistant professor and later became an adjunct professor.

In 2018, he received the Asan Award in Medicine for Young Medical Scientists from the Asan Foundation and the National R&D Excellence 100 from the Ministry of Science and ICT.

Introduction
graphic image for Research Center

Integrative Research on Structure and Function of various Leucine-Rich Repeat (LRR)-containing Proteins

  • - Identifying novel binding targets for LRR-containing proteins
  • - Determining 3D structure of LRR-containing proteins in complex with novel binding targets and their supramolecular signaling complexes using Cryo-EM and X-ray crystallography
  • - Investigating the molecular and cellular mechanism of LRR-containing proteins
  • - Uncovering the physiological and pathological roles of LRR-containing proteins
Main research activities

The knowledge gained from structural studies of biomolecules including protein domain, protein/protein, protein/DNA, and protein/RNA complexes, has significantly advanced our understanding on biological phenomena at the molecular level and has applied to the development of therapeutics. Since the structure of myoglobin was first determined in the 1950s by X-ray crystallography, this technique has been the most powerful tool in modern structural biology. Recent technical breakthroughs has led a resolution revolution in Cryo-EM and these achievements herald the beginning of a new era in the field of structural biology.


Our research group is undertaking innovative research to discover the novel binding targets of uncharacterized LRR-containing proteins and their cellular signaling network. These novel binding partners for uncharacterized LRR-containing proteins as well as the supramolecular signaling complexes will be the key targets for our structural research. To this end, our research group would like to establish four core facilities (Protein Expression core, high-performance Cryo-EM core, Protein Crystallization core, and Computing core for Cryo-EM image processing) at IBS Headquarter. We hope that our challenging approach will open a groundbreaking research field with the goal of expanding our understanding on the physiological and pathological roles of uncharacterized LRR-containing proteins. Moreover, the mechanistic insights from our integrative study on structure and function of various LRR-containing proteins can be also translated clinically in the form of diagnostic bio-markers as well as protein therapeutics. We are currently recruiting highly motivated young scientists with various academic backgrounds and offer them the best research environments.

Personnel
Personnel status
Total16
Gender7(Male), 9(Female)
Korean/ International15(Korean), 1(International)

As of February. 2020

Organization

Organization

Personnel
Personnel status
Total16
Gender7(Male), 9(Female)
Korean/ International15(Korean), 1(International)
Degree
Position

As of February. 2020

Research

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