Dr. Jeff Abramson
Membrane Protein Crystallography
53-254 CHS
310-825-3913
jabramson@mednet.ucla.edu
Visit my Lab
Research Interests:
Membrane transport proteins are responsible for many critical biological functions including governing energy transduction, modifying ion concentrations, and actively importing metabolites into the cell. Membrane proteins represent 20-30% of all proteins in each of the sequenced genomes. In addition, they are targets for 50% of all marketed drugs. Considering their biological and pharmacological relevance and their vast numbers throughout genomes, there is an enormous demand for structural information. However, membrane proteins represent only about ~0.7% of the protein structures in the Protein data bank. The reason for this discrepancy stems from the hydrophobic nature of membrane proteins, which reside in a phospholipid bilayer, making them difficult to express, purify, and crystallize.
Our lab is trying to overcome these barriers and resolve the structures of several channels and transporters. This is an ideal format for students to interact with other groups and learn numerous techniques through interdepartmental collaborations.
Representative Publications:
Ujwal R, Cascio D, Colletier JP, Faham S, Zhang J, Toro L, Ping P, Abramson J. The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating. Proc Natl Acad Sci U S A. 2008 Nov 18;105(46):17742-7.
Faham S, Watanabe A, Besserer GM, Cascio D, Specht A, Hirayama BA, Wright EM, Abramson J. The crystal structure of a sodium galactose transporter reveals mechanistic insights into Na+/sugar symport. Science. 2008 Aug 8;321(5890):810-4.
Abramson J, Smirnova I, Kasho V, Verner G, Kaback HR, Iwata S. (2003)
Structure and mechanism of the lactose permease of Escherichia coli. Science.;301(5633):610-5.
