Nicholas Levinson, PhD
3-121 Nils Hasselmo Hall
312 Church St SE
Minneapolis, MN 55455
United States
Dr. Levinson is an Associate Professor in the Department of Pharmacology and a member of the Masonic Cancer Center’s Genetic Mechanisms Program. Dr. Levinson received his Bachelors and Masters degrees in Biochemistry from Cambridge University, and his PhD degree from the University of California, Berkeley, where he studied the structural basis of protein kinase function. After postdoctoral training at Stanford University in the Department of Chemistry, he joined the University of Minnesota as an Assistant Professor in 2014.
Expertise
Protein kinase structural dynamics and allostery, kinase inhibitor targeting, protein crystallography, magnetic resonance, infrared spectroscopy and ultrafast fluorescence spectroscopy
Awards & Recognition
NIH R33 Grant CA246363, 2020
Medical School’s Faculty Research Development Grant, 2019
Dean’s first-R01 Award, UMN Medical School 130th Anniversary, 2018
NIH R01 Grant GM121515 2017
NIH R21 Grant CA217695 2017
NIH K99 Pathway to Independence Award, 2012-2017
NIH NRSA F32 Award, 2009-2011
Education
Associate Professor, Department of Pharmacology
Faculty, PhD Program in Biochemistry, Molecular Biology and Biophysics
Faculty, MS and PhD Programs in Pharmacology
Preceptor, Medical Scientist Training Program (Combined MD/PhD Training Program)
PhD, University of California, Berkeley
Research
Research Summary/Interests
The Levinson Lab studies the structural and dynamic basis for protein kinase function. We use a diversified range of methods spanning crystallography, magnetic resonance, and ultrafast spectroscopy to dissect the role of kinase conformational dynamics in catalytic function and drug targeting. Our work has revealed the existence of dynamic water networks in kinase active sites that are important for catalytic function, and shown that large-scale conformational changes play a critical role in selective recognition of kinase inhibitor drugs. We have also shown that kinase engagement with different regulatory partners modulates these dynamic effects to alter inhibitor recognition. We aim to leverage these approaches and insights for the design of next-generation cancer therapeutics that modulate kinase allosteric functions by tuning conformational dynamics.