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.
Cells produce a variety of ABC transporter proteins that shuttle numerous molecules across the plasma membrane so as to maintain the integrity of the intracellular milieu. As Higgins and Linton discuss in their Perspective, the first high-resolution crystal structure of one of these intricate ABC transporters has now been obtained (Chang and Roth). As the Perspective authors note, although the structure confirms much of the existing biochemical evidence, it also yields some interesting surprises that it will take much more analysis to explain.
The authors are at the MRC Clinical Sciences Centre, Imperial College School of Medicine, Hammersmith Hospital Campus, DuCane Road, London W12 0NN, UK. E-mail: christopher.higgins{at}csc.mrc.ac.uk
Mutational analysis of the yeast multidrug resistance ABC transporter Pdr5p with altered drug specificity.
A. C. Tutulan-Cunita, M. Mikoshi, M. Mizunuma, D. Hirata, and T. Miyakawa (2005)
Genes Cells
10, 409-420
|Abstract »|Full Text »|PDF »
Molecular Analysis of Resistance to Streptogramin A Compounds Conferred by the Vga Proteins of Staphylococci.
O. Chesneau, H. Ligeret, N. Hosan-Aghaie, A. Morvan, and E. Dassa (2005)
Antimicrob. Agents Chemother.
49, 973-980
|Abstract »|Full Text »|PDF »
Structures and Models of Transporter Proteins.
S. G. Dahl, I. Sylte, and A. W. Ravna (2004)
J. Pharmacol. Exp. Ther.
309, 853-860
|Abstract »|Full Text »|PDF »
The Role of FhuD2 in Iron(III)-Hydroxamate Transport in Staphylococcus aureus: DEMONSTRATION THAT FhuD2 BINDS IRON(III)-HYDROXAMATES BUT WITH MINIMAL CONFORMATIONAL CHANGE AND IMPLICATION OF MUTATIONS ON TRANSPORT.
M. T. Sebulsky, B. H. Shilton, C. D. Speziali, and D. E. Heinrichs (2003)
J. Biol. Chem.
278, 49890-49900
|Abstract »|Full Text »|PDF »
A Structural Model for the Open Conformation of the mdr1 P-glycoprotein Based on the MsbA Crystal Structure.
M. Seigneuret and A. Garnier-Suillerot (2003)
J. Biol. Chem.
278, 30115-30124
|Abstract »|Full Text »|PDF »
The Dynamic Dimerization of the Yeast ADP/ATP Carrier in the Inner Mitochondrial Membrane Is Affected by Conserved Cysteine Residues.
S. D. Dyall, S. C. Agius, C. De Marcos Lousa, V. Trezeguet, and K. Tokatlidis (2003)
J. Biol. Chem.
278, 26757-26764
|Abstract »|Full Text »|PDF »
RLIP76, a Novel Transporter Catalyzing ATP-Dependent Efflux of Xenobiotics.
S. Awasthi, R. Sharma, S. S. Singhal, P. Zimniak, and Y. C. Awasthi (2002)
Drug Metab. Dispos.
30, 1300-1310
|Abstract »|Full Text »|PDF »
