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Difficult dance steps: Team learns how membrane transporter moves
Date:12/2/2013

CHAMPAIGN, Ill. Researchers have tried for decades to understand the undulations and gyrations that allow transport proteins to shuttle molecules from one side of a cell membrane to the other. Now scientists report that they have found a way to penetrate the mystery. They have worked out every step in the molecular dance that enables one such transporter to do its job.

The new findings, reported in the Proceedings of the National Academy of Sciences, will help scientists figure out how other transporters work. The work also offers new insights into multi-drug-resistant (MDR) cancers, some of which use these transporters to export cancer-killing drugs. (Watch a video about the research that includes an animation of the transport protein in action.)

The transporter in the study, MsbA, belongs to an ancient family of proteins that carry large molecules across membranes. It is the bacterial version of a transporter in human cells (called p-glycoprotein) that helps pump drugs out of the cell, said Emad Tajkhorshid, a University of Illinois professor of biochemistry and of pharmacology who led the research. P-glycoprotein is overexpressed in some cancer cells, helping the cells eject drugs meant to kill them.

"There is a lot of research going on in pharmaceutical companies trying to find an inhibitor of p-glycoprotein," Tajkhorshid said. "If we can understand the transport cycle, we have a much larger repertoire of structures for rational drug design."

Research on large, membrane-bound proteins like MsbA has always been problematic because they are not easy to crystallize (a common technique for determining a protein's three-dimensional shape) and each crystal structure reflects only one of the many c
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Contact: Diana Yates
diya@illinois.edu
217-333-5802
University of Illinois at Urbana-Champaign
Source:Eurekalert  

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