5dhy: Difference between revisions
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==HIV-1 Rev NTD dimers with variable crossing angles== | |||
<StructureSection load='5dhy' size='340' side='right' caption='[[5dhy]], [[Resolution|resolution]] 3.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5dhy]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DHY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DHY FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dhv|5dhv]], [[5dhx|5dhx]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5dhy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dhy OCA], [http://pdbe.org/5dhy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dhy RCSB], [http://www.ebi.ac.uk/pdbsum/5dhy PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
HIV-1 Rev protein mediates the nuclear export of viral RNA genomes. To do so, Rev oligomerizes cooperatively onto an RNA motif, the Rev response element (RRE), forming a complex that engages with the host nuclear export machinery. To better understand Rev oligomerization, we determined four crystal structures of Rev N-terminal domain dimers, which show that they can pivot about their dyad axis, giving crossing angles of 90 degrees to 140 degrees . In parallel, we performed cryoelectron microscopy of helical Rev filaments. Filaments vary from 11 to 15 nm in width, reflecting variations in dimer crossing angle. These structures contain additional density, indicating that C-terminal domains become partially ordered in the context of filaments. This conformational variability may be exploited in the assembly of RRE/Rev complexes. Our data also revealed a third interface between Revs, which offers an explanation for how the arrangement of Rev subunits adapts to the "A"-shaped architecture of the RRE in export-active complexes. | |||
The Structure of HIV-1 Rev Filaments Suggests a Bilateral Model for Rev-RRE Assembly.,DiMattia MA, Watts NR, Cheng N, Huang R, Heymann JB, Grimes JM, Wingfield PT, Stuart DI, Steven AC Structure. 2016 May 31. pii: S0969-2126(16)30076-4. doi:, 10.1016/j.str.2016.04.015. PMID:27265851<ref>PMID:27265851</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Grimes, J | <div class="pdbe-citations 5dhy" style="background-color:#fffaf0;"></div> | ||
[[Category: Steven, A | == References == | ||
[[Category: Watts, N | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: DiMattia, M A]] | ||
[[Category: Grimes, J M]] | |||
[[Category: Steven, A C]] | |||
[[Category: Stuart, D I]] | |||
[[Category: Watts, N R]] | |||
[[Category: Wingfield, P T]] | |||
[[Category: Helical hairpin]] | |||
[[Category: Hiv]] | |||
[[Category: Immune system]] | |||
[[Category: Nuclear export]] | |||
[[Category: Rna-binding]] | |||
Revision as of 02:13, 24 June 2016
HIV-1 Rev NTD dimers with variable crossing anglesHIV-1 Rev NTD dimers with variable crossing angles
Structural highlights
Publication Abstract from PubMedHIV-1 Rev protein mediates the nuclear export of viral RNA genomes. To do so, Rev oligomerizes cooperatively onto an RNA motif, the Rev response element (RRE), forming a complex that engages with the host nuclear export machinery. To better understand Rev oligomerization, we determined four crystal structures of Rev N-terminal domain dimers, which show that they can pivot about their dyad axis, giving crossing angles of 90 degrees to 140 degrees . In parallel, we performed cryoelectron microscopy of helical Rev filaments. Filaments vary from 11 to 15 nm in width, reflecting variations in dimer crossing angle. These structures contain additional density, indicating that C-terminal domains become partially ordered in the context of filaments. This conformational variability may be exploited in the assembly of RRE/Rev complexes. Our data also revealed a third interface between Revs, which offers an explanation for how the arrangement of Rev subunits adapts to the "A"-shaped architecture of the RRE in export-active complexes. The Structure of HIV-1 Rev Filaments Suggests a Bilateral Model for Rev-RRE Assembly.,DiMattia MA, Watts NR, Cheng N, Huang R, Heymann JB, Grimes JM, Wingfield PT, Stuart DI, Steven AC Structure. 2016 May 31. pii: S0969-2126(16)30076-4. doi:, 10.1016/j.str.2016.04.015. PMID:27265851[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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