| Literature DB >> 11172724 |
J Marcotrigiano1, I B Lomakin, N Sonenberg, T V Pestova, C U Hellen, S K Burley.
Abstract
The X-ray structure of the phylogenetically conserved middle portion of human eukaryotic initiation factor (eIF) 4GII has been determined at 2.4 A resolution, revealing a crescent-shaped domain consisting of ten alpha helices arranged as five HEAT repeats. Together with the ATP-dependent RNA helicase eIF4A, this HEAT domain suffices for 48S ribosomal complex formation with a picornaviral RNA internal ribosome entry site (IRES). Structure-based site-directed mutagenesis was used to identify two adjacent features on the surface of this essential component of the translation initiation machinery that, respectively, bind eIF4A and a picornaviral IRES. The structural and biochemical results provide mechanistic insights into both cap-dependent and cap-independent translation initiation.Entities:
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Year: 2001 PMID： 11172724 DOI： 10.1016/s1097-2765(01)00167-8
Source DB: PubMed Journal: Mol Cell ISSN： 1097-2765 Impact factor: 17.970