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Jungsan Sohn, Ph.D.
Assistant Professor of Biophysics and Biophysical Chemistry
Research Interests: Use of mechanistic enzymology and X-ray crystallography to study allosterically regulated biological stress-sensors.
Dr. Jungsan (Jay) Sohn is an assistant professor of biophysics and biophysical chemistry at the Johns Hopkins University School of Medicine.
He received his B.S. from the University of Michigan in 2001, completed his Ph.D. at Duke University in 2008 and joined the faculty of Johns Hopkins in early 2011.
In his research, Dr. Sohn uses mechanistic enzymology and x-ray crystallography to study allosterically regulated biological stress-sensors with the purpose of understanding how they are assembled, how they detect danger signals and how they initiate stress-response.
He has authored or co-authored several peer-reviewed publications.
- Assistant Professor of Biophysics and Biophysical Chemistry
Departments / Divisions
- B.S., University of Michigan (Ann Arbor) (Michigan) (2001)
- Ph.D., Duke University (North Carolina) (2006)
Research & Publications
Innate immunity is the first line of defense against invading pathogens in higher eukaryotes. The central players of this well-conserved form of immune response are pattern-recognition receptors (PRRs) that can recognize pathogen associated molecular patterns (PAMPs) and danger-associated molecular patterns (DAMPs). NOD-like receptors (NLRs) are important PRRs of innate immunity. Notably, upon binding PAMP/DAMP and nucleosie-triphosphates (NTP), NLRs assemble into multi-protein complexes called inflammasomes. The assembled inflammasomes then transduce upstream signals to directly activate procaspase-1. The activated caspase-1 then facilitates maturation of inflammatory cytokines via proteolysis. The Sohn Lab asks the following questions: What is the mechanism of inflammasome assembly? What is the mechanism of procaspase-1 activation by inflammasomes? What are the molecular mechanisms of inflammasome regulation by protein modulators?
Lab Website: Jungsan Sohn
Sohn J., Grant, R.A., Sauer, R.T. "Allostery is an intrinsic property of the protease domain of DegS: implications for enzyme function and evolution." J. Biol. Chem. 2010; 285, 34039-47.
Sohn J., Grant, R.A., Sauer, R.T. "OMP peptides activate the DegS protease by a relief of inhibition mechanism." Structure. 2009; 17:1411-21.
Sohn J. and Sauer, R.T. "OMP peptides modulate the activity of DegS protease by differential binding to active and inactive conformations." Molecular Cell. 2009; 33, 64-74.
Sohn J., Grant R.A., Sauer R.T. "Allosteric activation of DegS, a stress sensor PDZ-protease." Cell. 2007; 131, 572-583.
Academic Affiliations & Courses
Graduate Program Affiliation
Program in Molecular Biophysics