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.
GoGreen Membership

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Sci. STKE, 2 January 2007
Vol. 2007, Issue 367, p. tw5
[DOI: 10.1126/stke.3672007tw5]

EDITORS' CHOICE

Biochemistry News on Networking

L. Bryan Ray

Science, Science’s STKE, AAAS, Washington, DC 20005, USA

Analysis of large data sets describing protein interactions is helping to define how networks of protein interactions control cell function. Kim et al. analyze an improved data set that includes information on three-dimensional protein structure and protein domains, which allows distinctions to be made between particular interaction domains and clarifies, for example, whether interactions between two proteins containing the same domain with another protein are expected to be mutually exclusive. This analysis restricts the estimated maximal numbers of protein partners (14) compared with previous estimates. The number of interaction interfaces on a protein is a key defining factor in whether a protein is essential for cell function and for its evolutionary rate.

P. M. Kim, L. J. Lu, Y. Xia, M. B. Gerstein, Relating three-dimensional structures to protein networks provides evolutionary insights. Science 314, 1938-1941 (2006). [Abstract] [Full Text]

T. O. Yeates, M. Beeby, Proteins in a small world. Science 314, 1882-1883 (2006). [Summary] [Full Text]

Citation: L. B. Ray, News on Networking. Sci. STKE 2007, tw5 (2007).

ADVERTISEMENT
Click Me!

ADVERTISEMENT

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (pre-2008: Science's STKE. ISSN 1525-8882)