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1: Science. 2005 Dec 2;310(5753):1513-5.Click here to read Links
Comment in:
Hepatology. 2006 Dec;44(6):1687-90.

Structural roles for human translation factor eIF3 in initiation of protein synthesis.

Siridechadilok B, Fraser CS, Hall RJ, Doudna JA, Nogales E.

Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.

Protein synthesis in mammalian cells requires initiation factor eIF3, a approximately 750-kilodalton complex that controls assembly of 40S ribosomal subunits on messenger RNAs (mRNAs) bearing either a 5'-cap or an internal ribosome entry site (IRES). Cryo-electron microscopy reconstructions show that eIF3, a five-lobed particle, interacts with the hepatitis C virus (HCV) IRES RNA and the 5'-cap binding complex eIF4F via the same domain. Detailed modeling of eIF3 and eIF4F onto the 40S ribosomal subunit reveals that eIF3 uses eIF4F or the HCV IRES in structurally similar ways to position the mRNA strand near the exit site of 40S, promoting initiation complex assembly.

PMID: 16322461 [PubMed - indexed for MEDLINE]