Roland Dunbrack

Structural bioinformatics and structure prediction of all 494 human protein kinases and their interactions

Abstract: 

Humans have 493 human protein kinase domains with the typical kinase fold, divided into 437 catalytic protein kinases and 56 pseudokinases. We have used structural bioinformatics of substrate-bound kinase structures in the PDB to identify criteria for classifying active and various inactive forms of protein kinases. With AlphaFold2, we have used these criteria to model all 437 catalytic kinases in their active form. By clustering the inactive forms, we have modeled many human kinases in their most likely biologically relevant inactive form. Similar efforts on pseudokinases have established the most common conformations for each of them, which may be used to model interactions with other proteins.

Speaker: Roland Dunbrack, Fox Chase Cancer Center

Dr. Dunbrack grew up in Massachusetts and received his AB in Chemistry in 1985 and PhD in biophysics in 1993 at Harvard University. After a postdoctoral fellowship at UCSF in 1997, he started his lab at Fox Chase Cancer Center where he has remained ever since. He has been active in the field of structural bioinformatics of proteins and protein complexes and the development of protein structure prediction methods. He has contributed extensively to scoring function and algorithms in the program Rosetta. At Fox Chase, he directs the Molecular Modeling Facility which works with colleagues across the Center to apply protein structure prediction to problems in cancer biology.

Host: Jason Kahn

Seminars start at 4:00 pm, and refreshments will be served at 3:45 pm.

This seminar will be held in room 3150 of the Physical Sciences Complex (Bldg #415).