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.

Science 1 December 2006:
Vol. 314. no. 5804, p. 1349
DOI: 10.1126/science.314.5804.1349i
Prev | Table of Contents | Next

This Week in Science

Figure 1 The canonical mechanism for initiation of protein synthesis in eukaryotes involves a nucleotide cap on messenger RNA (mRNA) that is recognized by an initiation protein factor. However, a variety of pathogenic viruses and cellular mRNAs bypass the canonical mechanism by using structured RNA sequences, called internal ribosomal entry sites (IRESs), to initiate translation. Pfingsten et al. (p. 1450) have determined the structure of the ribosome-binding domain of an IRES at 3.1 angstrom resolution. The RNA prefolds to create a specific ribosome-binding structure. By docking the structure onto cryoelectron microscopic reconstructions of an IRES-ribosome complex, contacts were identified that drive binding and induce conformational change in the ribosome.

CREDIT: PFINGSTEN ET AL.




To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)