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Comparative sequence and structure analysis of eIF1A and eIF1AD

Overview of attention for article published in BMC Structural Biology, September 2018
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Title
Comparative sequence and structure analysis of eIF1A and eIF1AD
Published in
BMC Structural Biology, September 2018
DOI 10.1186/s12900-018-0091-6
Pubmed ID
Authors

Jielin Yu, Assen Marintchev

Abstract

Eukaryotic translation initiation factor 1A (eIF1A) is universally conserved in all organisms. It has multiple functions in translation initiation, including assembly of the ribosomal pre-initiation complexes, mRNA binding, scanning, and ribosomal subunit joining. eIF1A binds directly to the small ribosomal subunit, as well as to several other translation initiation factors. The structure of an eIF1A homolog, the eIF1A domain-containing protein (eIF1AD) was recently determined but its biological functions are unknown. Since eIF1AD has a known structure, as well as a homolog, whose structure and functions have been extensively studied, it is a very attractive target for sequence and structure analysis. Structure/sequence analysis of eIF1AD found significant conservation in the surfaces corresponding to the ribosome-binding surfaces of its paralog eIF1A, including a nearly invariant surface-exposed tryptophan residue, which plays an important role in the interaction of eIF1A with the ribosome. These results indicate that eIF1AD may bind to the ribosome, similar to its paralog eIF1A, and could have roles in ribosome biogenenesis or regulation of translation. We identified conserved surfaces and sequence motifs in the folded domain as well as the C-terminal tail of eIF1AD, which are likely protein-protein interaction sites. The roles of these regions for eIF1AD function remain to be determined. We have also identified a set of trypanosomatid-specific surface determinants in eIF1A that could be a promising target for development of treatments against these parasites. The results described here identify regions in eIF1A and eIF1AD that are likely to play major functional roles and are promising therapeutic targets. Our findings and hypotheses will promote new research and help elucidate the functions of eIF1AD.

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Mendeley readers

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Geographical breakdown

Country Count As %
Unknown 6 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 2 33%
Researcher 2 33%
Student > Bachelor 1 17%
Unknown 1 17%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 4 67%
Neuroscience 1 17%
Unknown 1 17%

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 06 September 2018.
All research outputs
#11,949,970
of 13,477,526 outputs
Outputs from BMC Structural Biology
#155
of 181 outputs
Outputs of similar age
#228,843
of 265,471 outputs
Outputs of similar age from BMC Structural Biology
#1
of 1 outputs
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