Crystal structure of an HIV assembly and maturation switch
eLife, ISSN: 2050-084X, Vol: 5, Issue: 2016JULY, Page: e17063
2016
- 114Citations
- 109Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations114
- Citation Indexes114
- CrossRef114
- 106
- Captures109
- Readers109
- 109
Article Description
Virus assembly and maturation proceed through the programmed operation of molecular switches, which trigger both local and global structural rearrangements to produce infectious particles. HIV-1 contains an assembly and maturation switch that spans the C-terminal domain (CTD) of the capsid (CA) region and the first spacer peptide (SP1) of the precursor structural protein, Gag. The crystal structure of the CTD-SP1 Gag fragment is a goblet-shaped hexamer in which the cup comprises the CTD and an ensuing type II β-turn, and the stem comprises a 6-helix bundle. The β-turn is critical for immature virus assembly and the 6-helix bundle regulates proteolysis during maturation. This bipartite character explains why the SP1 spacer is a critical element of HIV-1 Gag but is not a universal property of retroviruses. Our results also indicate that HIV-1 maturation inhibitors suppress unfolding of the CA-SP1 junction and thereby delay access of the viral protease to its substrate.
Bibliographic Details
10.7554/elife.17063; 10.7554/elife.17063.002; 10.7554/elife.17063.016; 10.7554/elife.17063.019; 10.7554/elife.17063.001; 10.7554/elife.17063.004; 10.7554/elife.17063.020; 10.7554/elife.17063.011; 10.7554/elife.17063.013; 10.7554/elife.17063.003; 10.7554/elife.17063.008; 10.7554/elife.17063.010
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84979645614&origin=inward; http://dx.doi.org/10.7554/elife.17063; http://www.ncbi.nlm.nih.gov/pubmed/27416583; https://elifesciences.org/articles/17063#digest; http://dx.doi.org/10.7554/elife.17063.002; https://elifesciences.org/articles/17063#tbl2; http://dx.doi.org/10.7554/elife.17063.016; https://elifesciences.org/articles/17063#decision-letter; http://dx.doi.org/10.7554/elife.17063.019; https://elifesciences.org/articles/17063#abstract; http://dx.doi.org/10.7554/elife.17063.001; https://elifesciences.org/articles/17063#fig1; http://dx.doi.org/10.7554/elife.17063.004; http://dx.doi.org/10.7554/elife.17063.020; https://elifesciences.org/articles/17063#fig4; http://dx.doi.org/10.7554/elife.17063.011; https://elifesciences.org/articles/17063#fig5; http://dx.doi.org/10.7554/elife.17063.013; https://elifesciences.org/articles/17063#tbl1; http://dx.doi.org/10.7554/elife.17063.003; https://elifesciences.org/articles/17063; https://elifesciences.org/articles/17063#fig2; http://dx.doi.org/10.7554/elife.17063.008; https://elifesciences.org/articles/17063#fig3; http://dx.doi.org/10.7554/elife.17063.010; https://cdn.elifesciences.org/articles/17063/elife-17063-v3.pdf; https://cdn.elifesciences.org/articles/17063/elife-17063-v3.xml; https://elifesciences.org/articles/17063#author-response; https://dx.doi.org/10.7554/elife.17063
eLife Sciences Organisation, Ltd.
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