7urt: Difference between revisions

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'''Unreleased structure'''


The entry 7urt is ON HOLD
==T=1 particle HIV-1 CA G60A/G61P/M66A==
<StructureSection load='7urt' size='340' side='right'caption='[[7urt]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7urt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7URT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7URT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.39&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7urt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7urt OCA], [https://pdbe.org/7urt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7urt RCSB], [https://www.ebi.ac.uk/pdbsum/7urt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7urt ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The HIV-1 capsid is a fullerene cone made of quasi-equivalent hexamers and pentamers of the viral CA protein. Typically, quasi-equivalent assembly of viral capsid subunits is controlled by a molecular switch. Here, we identify a Thr-Val-Gly-Gly motif that modulates CA hexamer/pentamer switching by folding into a 3(10) helix in the pentamer and random coil in the hexamer. Manipulating the coil/helix configuration of the motif allowed us to control pentamer and hexamer formation in a predictable manner, thus proving its function as a molecular switch. Importantly, the switch also remodels the common binding site for host factors that are critical for viral replication and the new ultra-potent HIV-1 inhibitor lenacapavir. This study reveals that a critical assembly element also modulates the post-assembly and viral replication functions of the HIV-1 capsid and provides new insights on capsid function and inhibition.


Authors: Pornillos, O., Ganser-Pornillos, B.K., Schirra, R.T.
A molecular switch modulates assembly and host factor binding of the HIV-1 capsid.,Schirra RT, Dos Santos NFB, Zadrozny KK, Kucharska I, Ganser-Pornillos BK, Pornillos O Nat Struct Mol Biol. 2023 Mar;30(3):383-390. doi: 10.1038/s41594-022-00913-5. , Epub 2023 Feb 9. PMID:36759579<ref>PMID:36759579</ref>


Description: T=1 particle HIV-1 CA G60A/G61P/M66A
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Pornillos, O]]
<div class="pdbe-citations 7urt" style="background-color:#fffaf0;"></div>
[[Category: Schirra, R.T]]
 
[[Category: Ganser-Pornillos, B.K]]
==See Also==
*[[Gag polyprotein 3D structures|Gag polyprotein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human immunodeficiency virus 1]]
[[Category: Large Structures]]
[[Category: Ganser-Pornillos BK]]
[[Category: Pornillos O]]
[[Category: Schirra RT]]

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