Natalia Jura

Professor




Website: https://cvri.ucsf.edu/~jura
Email: Natalia.Jura / ucsf, edu

555 Mission Bay Blvd South, Smith Cardiovascular Research Building, Room 452W
San Francisco, CA 94158

Phone: 415 514-1133

Dr. Jura is an Professor at the Department of Cellular and Molecular Pharmacology and an Investigator at the Cardiovascular Research Institute at the School of Medicine, University of California, San Francisco (UCSF). She is also an Associate Director of the Quantitative Biosciences Institute at UCSF. Dr. Jura received her M.S in biochemistry from Jagiellonian University in Krakow, Poland and her Ph.D. in molecular and cellular biology from Stony Brook University.

Dr. Jura’s group focuses on understanding how soluble protein kinases and membrane-associated receptor kinases assemble into functional complexes and regulate their signaling through molecular interactions with regulatory proteins. To accomplish this, Dr. Jura’s research combines experimental methods such as X-ray crystallography, cryo-EM, enzyme biochemistry, membrane reconstitution and cell-based signaling assays. Most of Dr. Jura’s group current efforts focus on Receptor Tyrosine Kinases (RTKs) that belong to the family of human epidermal growth factor receptors (HERs/ERBBs). HER receptors signal as growth factor-induced dimers and they are targets of mutations in several types of human cancers, including breast, lung and brain. Dr. Jura’s group solved the first crystal structure of the HER3 kinase and of its heterotypic complex with EGFR, elucidating the molecular basis for their heterodimerization and mechanisms of action of HER3 cancer mutations. Most recently, using cryo-EM her group solved first structures of the HER2/HER3 complex bound to a growth factor, neuregulin, and therapeutic antibody trastuzumab (Herceptin).

Dr. Jura’s group also investigates alternative non-catalytic roles of protein kinases as scaffolds in cellular signaling pathways and applies this knowledge for design of small molecule inhibitors that target these poorly understood kinase functions in human diseases. Her group discovered a new pseudokinase in the human genome, PEAK3, and has contributed to the molecular understanding of signaling by the Tribbles (TRIB) family of pseudokinases.