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. Signal., 18 January 2011
Vol. 4, Issue 156, p. ec22
[DOI: 10.1126/scisignal.4156ec22]

EDITORS' CHOICE

Biochemistry Controlling Inflammation

Valda Vinson

Science, AAAS, Washington, DC 20005, USA

Lipids that mediate the inflammatory response are synthesized from arachidonic acid by the enzyme 5-lipoxygenase (5-LOX). An intrinsic instability of 5-LOX has been proposed to regulate its activity. Structures of related enzymes have shown that the C terminus penetrates the enzyme so that the main chain carboxylate of the C-terminal residue binds the catalytic iron. Gilbert et al. identified a sequence that probably destabilizes the orientation of the C terminus in 5-LOX and, by substituting this sequence, were able to purify a stable enzyme and determine its crystal structure. The structure is consistent with the proposed mechanism of enzyme inactivation and provides a basis for the design of 5-LOX–specific inhibitors.

N. C. Gilbert, S. G. Bartlett, M. T. Waight, D. B. Neau, W. E. Boeglin, A. R. Brash, M. E. Newcomer, The structure of human 5-lipoxygenase. Science 331, 217–219 (2011). [Abstract] [Full Text]

Citation: V. Vinson, Controlling Inflammation. Sci. Signal. 4, ec22 (2011).

To Advertise     Find Products

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