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.


Sci. STKE, 27 March 2001
Vol. 2001, Issue 75, p. tw10
[DOI: 10.1126/stke.2001.75.tw10]

EDITORS' CHOICE

Structural Biology Exploiting a Preexisting Condition

Phosphorylation is usually assumed to regulate signal transduction by triggering a conformational switch. Volkman et al. show that in the signaling protein NtrC, activation by phosphorylation involves stabilization of a preexisting conformation. Nuclear magnetic resonance measurements of backbone dynamics show that both active and inactive conformations are populated in unphosphorylated NtrC, with the inactive form favored. Phosphorylation shifts the equilibrium far toward the active conformation, so that conformational exchange virtually disappears. Thus, allosteric regulation of single domains may be important in signal transduction. Buck and Rosen provide a Perspective on the data.

B. F. Volkman, D. Lipson, D. E. Wemmer, D. Kern, Two-state allosteric behavior in a single-domain signaling protein. Science 291, 2429-2433 (2001). [Abstract] [Full Text]

M. Buck, M. K. Rosen, Flipping a switch. Science 291, 2329-2330 (2001). [Full Text]

Citation: Exploiting a Preexisting Condition. Sci. STKE 2001, tw10 (2001).


To Advertise     Find Products


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