Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
The translation initiation factor eIF1A is necessary for directing the 43S preinitiation complex from the 5' end of the mRNA to the initiation codon in a process termed scanning. We have determined the solution structure of human eIF1A, which reveals an oligonucleotide-binding (OB) fold and an additional domain. NMR titration experiments showed that eIF1A binds single-stranded RNA oligonucleotides in a site-specific, but non-sequence-specific manner, hinting at an mRNA interaction rather than specific rRNA or tRNA binding. The RNA binding surface extends over a large area covering the canonical OB fold binding site as well as a groove leading to the second domain. Site-directed mutations at multiple positions along the RNA-binding surface were defective in the ability to properly assemble preinitiation complexes at the AUG codon in vitro.
The eIF1A solution structure reveals a large RNA-binding surface important for scanning function.,Battiste JL, Pestova TV, Hellen CU, Wagner G Mol Cell. 2000 Jan;5(1):109-19. PMID:10678173[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Battiste JL, Pestova TV, Hellen CU, Wagner G. The eIF1A solution structure reveals a large RNA-binding surface important for scanning function. Mol Cell. 2000 Jan;5(1):109-19. PMID:10678173
