1d7q: Difference between revisions
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'''HUMAN TRANSLATION INITIATION FACTOR EIF1A'''<br /> | '''HUMAN TRANSLATION INITIATION FACTOR EIF1A'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1D7Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1D7Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D7Q OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: rna-binding protein]] | [[Category: rna-binding protein]] | ||
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Revision as of 16:38, 15 February 2008
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HUMAN TRANSLATION INITIATION FACTOR EIF1A
OverviewOverview
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.
About this StructureAbout this Structure
1D7Q is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
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