Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 13 May 2005:
Vol. 308. no. 5724, pp. 963 - 965
DOI: 10.1126/science.1113414
Prev | Table of Contents | Next

Perspectives

STRUCTURAL BIOLOGY:
Flipping Lipids: Is the Third Time the Charm?

Amy L. Davidson and Jue Chen

Certain membrane-spanning proteins expel hydrophobic molecules such as lipids and drugs from cells, but just how they accomplish this has been unclear. As Davidson and Chen describe in their Perspective, two new studies (Dong et al., and Reyes et al.) explain how a transporter protein called MsbA expends energy and changes its organization to flip a molecule from one side of the membrane to the other.

A. L. Davidson is in the Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX 77030, USA. E-mail: davidson{at}bcm.tmc.edu J. Chen is in the Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA. E-mail: chenjue{at}purdue.edu

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
On Parallel and Antiparallel Topology of a Homodimeric Multidrug Transporter.
M. Soskine, S. Mark, N. Tayer, R. Mizrachi, and S. Schuldiner (2006)
J. Biol. Chem. 281, 36205-36212
   Abstract »    Full Text »    PDF »
Functional Importance of Three Basic Residues Clustered at the Cytosolic Interface of Transmembrane Helix 15 in the Multidrug and Organic Anion Transporter MRP1 (ABCC1).
G. Conseil, R. G. Deeley, and S. P. C. Cole (2006)
J. Biol. Chem. 281, 43-50
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)