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 ~0.6% (218 out of 38479) of the protein structures in the Protein data bank (PDB August 2006). 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:
Nicoll DA, Sawaya MR, Kwon S, Cascio D, Philipson KD, Abramson J.(2006)
The crystal structure of the primary Ca2+ sensor of the Na+/Ca2+ exchanger reveals a novel Ca2+ binding motif.
J Biol Chem. 4;281(31).
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.
Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M. (2000)
The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site.
Nat Struct Biol. (10):910-7.
