Box 951737
BSRB 330
615 Charles E. Young Drive South
Los Angeles, CA 90095
Boyer Hall room 356 611 Charles E Young Drive East
Los Angeles, CA 90095
Membrane proteins constitute about 30% of all genome-encoded proteins and are targets for over 40% of all drugs in use today. While the number of membrane protein structure increases, providing valuable insights into their architecture and function, the molecular mechanisms governing their proper localization, assembly and insertion into biological membranes still remain elusive. Protein export and secretion is essential to life and all living cells have developed sophisticated machineries and subtle regulation mechanisms, and spend considerable energy to ensure proper targeting, folding and assembly of this particular class of proteins.
We are interested in the study of different membrane protein targeting and translocation systems in all three kingdoms of life (Bacteria, Archea and, Eukarya) and we primarily use X-ray crystallography in combination with other biophysical techniques to unravel the general molecular mechanisms that govern the proper targeting, folding and insertion of membrane proteins. On the long-term, we also seek to develop inhibitors of these systems that could be used as anti-bacterial, anti-fungal, anti-parasitic and anti-cancer drugs.
Membrane Protein Folding, Targeting, and Assembly.
Structure of Macromolecular Complexes.
Macromolecular Complexes: Membrane Protein and Protein-RNA Complexes.
Structural Biology: X-ray crystallography and Solution Biophysics.
Membrane proteins constitute about 30% of all genome-encoded proteins and are targets for over 40% of all drugs in use today. While the number of membrane protein structure increases, providing valuable insights into their architecture and function, the molecular mechanisms governing their proper localization, assembly and insertion into biological membranes still remain elusive. Protein export and secretion is essential to life and all living cells have developed sophisticated machineries and subtle regulation mechanisms, and spend considerable energy to ensure proper targeting, folding and assembly of this particular class of proteins.
We are interested in the study of different membrane protein targeting and translocation systems in all three kingdoms of life (Bacteria, Archea and, Eukarya) and we primarily use X-ray crystallography in combination with other biophysical techniques to unravel the general molecular mechanisms that govern the proper targeting, folding and insertion of membrane proteins. On the long-term, we also seek to develop inhibitors of these systems that could be used as anti-bacterial, anti-fungal, anti-parasitic and anti-cancer drugs.
Pascal Egea received is B.S. in Molecular and Cellular Biology from the Ecole Normale Supérieure de Lyon (Lyon, France) in 1991. He then went to graduate school at the Université Louis Pasteur (Strasbourg, France) where he studied the structure and function of the retinoic acid receptors in the laboratory of Dr Dino Moras. After completing is Ph.D. in 1999, Pascal went to the University of California in San Francisco for post-doctoral training under the co-mentorship of Professors Robert Stroud and Peter Walter; during this period he studied the signal recognition particle and protein translocation pathways. Pascal joined the Department of Biological Chemistry as an assistant professor in the fall of 2009.
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