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Jae-Hyun Cho

Cho, Jae-Hyun
Jae-Hyun Cho
Assistant Professor of Biochemistry and Biophysics
NMR / N113A
Undergraduate Education
B.S., Biology, Han-Yang University, South Korea 1997
Graduate Education
M.S., Protein Engineering, Pohang University of Science and Technology, South Korea 1999
Ph.D SUNY-Stonybrook 2006
Postdoc: Columbia University
Joined Texas A&M in 2012

Structural dynamics of multi-domain signaling proteins

The importance of understanding the regulatory mechanism of the intra-molecular interactions is highlighted by the observation that nearly 65%-80% of eukaryotic proteins consist of multiple domains. The multidomain architecture generates “emergent properties” that are not demonstrated by their individual domains and should be investigated in the context of full-length protein. In these systems, the dynamics of the intra-molecular interactions between domains provides fundamental mechanisms for many biological processes such as autoinhibition, allosteric modulation of kinase activity and molecular recognition of target proteins.

Two closely related multidomain proteins, the signaling adaptor protein Crk-II and cAbl kinase, will be targeted to delineate the underlying regulatory mechanism of intra- and inter-molecular protein-protein interactions. Dysregulation of the intramolecular interdomain interactions in Crk-II and cAbl kinase are closely associated with cancer and pathogen infection.

Our research interests lie in the interface between biology and other areas of science (chemistry and physics). NMR is our primary tool for structural and biophysical analysis. We also extensively use other techniques including Circular Dichroism and Fluorescence spectroscopy, and Isothermal calorimetry. These biophysical analyses are corroborated by sophisticated engineering and tuning of target proteins using semi-synthetic chemical biology techniques, in addition to traditional molecular biology methods.


Recent Publications

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  1. Shi, J, Shen, Q, Cho, JH, Hwang, W. Entropy Hotspots for the Binding of Intrinsically Disordered Ligands to a Receptor Domain. Biophys. J. 2020;118 (10):2502-2512.
    doi: 10.1016/j.bpj.2020.03.026. PubMed PMID:32311315. PubMed Central PMC7231926.

  2. Dubrow, A, Lin, S, Savage, N, Shen, Q, Cho, JH. Molecular Basis of the Ternary Interaction between NS1 of the 1918 Influenza A Virus, PI3K, and CRK. Viruses. 2020;12 (3):.
    doi: 10.3390/v12030338. PubMed PMID:32244879. PubMed Central PMC7150778.

  3. Cho, JH, Zhao, B, Shi, J, Savage, N, Shen, Q, Byrnes, J et al.. Molecular recognition of a host protein by NS1 of pandemic and seasonal influenza A viruses. Proc. Natl. Acad. Sci. U.S.A. 2020;117 (12):6550-6558.
    doi: 10.1073/pnas.1920582117. PubMed PMID:32152123. PubMed Central PMC7104383.

  4. Shen, Q, Cho, JH. The structure and conformational plasticity of the nonstructural protein 1 of the 1918 influenza A virus. Biochem. Biophys. Res. Commun. 2019;518 (1):178-182.
    doi: 10.1016/j.bbrc.2019.08.027. PubMed PMID:31420169. PubMed Central PMC6717002.

  5. Shen, Q, Bhatt, VS, Krieger, I, Sacchettini, JC, Cho, JH. Structure-guided design of a potent peptide inhibitor targeting the interaction between CRK and ABL kinase. Medchemcomm. 2018;9 (3):519-524.
    doi: 10.1039/c7md00619e. PubMed PMID:30108942. PubMed Central PMC6072116.

  6. Shen, Q, Shi, J, Zeng, D, Zhao, B, Li, P, Hwang, W et al.. Molecular Mechanisms of Tight Binding through Fuzzy Interactions. Biophys. J. 2018;114 (6):1313-1320.
    doi: 10.1016/j.bpj.2018.01.031. PubMed PMID:29590589. PubMed Central PMC5883614.

  7. Sato, S, Cho, JH, Peran, I, Soydaner-Azeloglu, RG, Raleigh, DP. The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State. Biophys. J. 2017;112 (9):1797-1806.
    doi: 10.1016/j.bpj.2017.01.034. PubMed PMID:28494951. PubMed Central PMC5425357.

  8. Shen, Q, Zeng, D, Zhao, B, Bhatt, VS, Li, P, Cho, JH et al.. The Molecular Mechanisms Underlying the Hijack of Host Proteins by the 1918 Spanish Influenza Virus. ACS Chem. Biol. 2017;12 (5):1199-1203.
    doi: 10.1021/acschembio.7b00168. PubMed PMID:28368102. .

  9. Zeng, D, Shen, Q, Cho, JH. Thermodynamic contribution of backbone conformational entropy in the binding between SH3 domain and proline-rich motif. Biochem. Biophys. Res. Commun. 2017;484 (1):21-26.
    doi: 10.1016/j.bbrc.2017.01.089. PubMed PMID:28111343. .

  10. Zeng, D, Bhatt, VS, Shen, Q, Cho, JH. Kinetic Insights into the Binding between the nSH3 Domain of CrkII and Proline-Rich Motifs in cAbl. Biophys. J. 2016;111 (9):1843-1853.
    doi: 10.1016/j.bpj.2016.09.029. PubMed PMID:27806266. PubMed Central PMC5103021.

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