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.

Subscribe

Sci. Signal., 2 September 2008
Vol. 1, Issue 35, p. ec313
[DOI: 10.1126/scisignal.135ec313]

EDITORS' CHOICE

Structural Biology VDAC-1 Structure in Solution

Valda J. Vinson

Science, AAAS, Washington, DC 20005, USA

In eukaryotes, a voltage-dependent anion channel (VDAC) facilitates diffusion of metabolites across the mitochondrial outer membrane. Closure of the human isoform, VDAC-1, leads to mitochondrial apoptosis. Hiller et al. have determined the nuclear magnetic resonance solution structure of VDAC-1 in detergent micelles. Whereas known beta barrel structures have an even number of strands, VDAC-1 has a 19-stranded barrel with parallel pairing of the first and last strands. Chemical shift data were used to map interaction sites for the substrates NADH and cholesterol and for the antiapoptotic protein Bcl-xL that opens the channel and thus inhibits apoptosis. The structure provides a framework for reanalysis of existing biochemical and biophysical data.

S. Hiller, R. G. Garces, T. J. Malia, V. Y. Orekhov, M. Colombini, G. Wagner, Solution structure of the integral human membrane protein VDAC-1 in detergent micelles. Science 321, 1206-1210 (2008). [Abstract] [Full Text]

Citation: V. J. Vinson, VDAC-1 Structure in Solution. Sci. Signal. 1, ec313 (2008).


To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882