View source for 30of


==HIV-1 capsid tri-hexamer bound to MX2==
<StructureSection load='30of' size='340' side='right'caption='[[30of]], [[Resolution|resolution]] 4.64&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[30of]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/HIV-1_group_M HIV-1 group M], [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=30OF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=30OF 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]] 4.64&#8491;</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=30of FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=30of OCA], [https://pdbe.org/30of PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=30of RCSB], [https://www.ebi.ac.uk/pdbsum/30of PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=30of ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C9JS04_HUMAN C9JS04_HUMAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The HIV-1 capsid core encapsulates the viral genome and mediates its delivery into the host cell's nucleus. It is composed of multiple copies of the Capsid (CA, p24(Gag)) protein, assembled into hexamers and pentamers to create a lattice that forms a fullerene-like cone. Myxovirus resistance 2 (MX2) is an HIV-1 restriction factor that binds to the capsid core and blocks nuclear import of the viral genome. Here, we define a minimal region of MX2 required for HIV-1 restriction and produce a corresponding functional recombinant protein. We have used cryo-electron microscopy to determine the structure of this MX2 fragment bound to the tri-hexamer interface of the capsid lattice, revealing a large, buried interface combining electrostatic and hydrophobic interactions. This structure, together with assays that measure capsid core destabilisation, shows that MX2 binding induces conformational rearrangements in the capsid lattice that culminate in a loss of integrity. These results support a model whereby MX2 exerts its antiviral activity by disrupting the capsid lattice, inducing premature fragmentation and preventing HIV-1 nuclear import. By revealing the structural basis for MX2-mediated restriction, this work also provides the framework for the development of anti-HIV molecules that mimic MX2 restriction.

MX2 Mediates Collapse of the HIV-1 Capsid.,Goodale A, Huang SW, Almeida N, Williamson DJ, Shkriabai N, Betancor G, Apolonia L, DiMaio F, Padilla-Parra S, Kvaratskhelia M, Bergeron JRC, Malim MH bioRxiv [Preprint]. 2026 May 8:2026.05.07.723526. doi: , 10.64898/2026.05.07.723526. PMID:42146390<ref>PMID:42146390</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 30of" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: HIV-1 group M]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Bergeron JRC]]
[[Category: DiMaio F]]
[[Category: Goodale A]]