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, 18 September 2007
Vol. 2007, Issue 404, p. tw340
[DOI: 10.1126/stke.4042007tw340]

EDITORS' CHOICE

Protein Structure Functional Evolution of Proteins

Valda J. Vinson

Science, AAAS, Washington, DC 20005, USA

The direct identification of protein evolution mechanisms requires comparing proteins through evolutionary time. The sequence of the 450-million-year-old ancestor of vertebrate mineralocorticoid (MR) and glucocorticoid (GR) receptors was previously determined by phylogenetic analysis, and the ancestor was shown to have MR-like hormone specificity. Ortlund et al. used structural, functional, and phylogenetic analysis to determine how specific mutations resulted in a change from MR-like to GR hormone specificity. They find evidence for epistatic interactions where a substitution changed the conformation at another site. Substitutions that had no immediate functional effect, but affected stability to allow subsequent function-switching mutations, played an important role in GR evolution.

E. A. Ortlund, J. T. Bridgham, M. R. Redinbo, J. W. Thornton, Crystal structure of an ancient protein: Evolution by conformational epistasis. Science 317, 1544-1548 (2007). [Abstract] [Full Text]

Citation: V. J. Vinson, Functional Evolution of Proteins. Sci. STKE 2007, tw340 (2007).

To Advertise     Find Products

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