View source for 5hgk


==HIV-1 CA N-terminal domain, open conformation==
<StructureSection load='5hgk' size='340' side='right'caption='[[5hgk]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5hgk]] is a 2 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=5HGK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HGK FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.763&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=5hgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hgk OCA], [https://pdbe.org/5hgk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hgk RCSB], [https://www.ebi.ac.uk/pdbsum/5hgk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hgk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A9PKC6_9HIV1 A9PKC6_9HIV1] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
During the early stages of infection, the HIV-1 capsid protects viral components from cytosolic sensors and nucleases such as cGAS and TREX, respectively, while allowing access to nucleotides for efficient reverse transcription. Here we show that each capsid hexamer has a size-selective pore bound by a ring of six arginine residues and a 'molecular iris' formed by the amino-terminal beta-hairpin. The arginine ring creates a strongly positively charged channel that recruits the four nucleotides with on-rates that approach diffusion limits. Progressive removal of pore arginines results in a dose-dependent and concomitant decrease in nucleotide affinity, reverse transcription and infectivity. This positively charged channel is universally conserved in lentiviral capsids despite the fact that it is strongly destabilizing without nucleotides to counteract charge repulsion. We also describe a channel inhibitor, hexacarboxybenzene, which competes for nucleotide binding and efficiently blocks encapsidated reverse transcription, demonstrating the tractability of the pore as a novel drug target.

HIV-1 uses dynamic capsid pores to import nucleotides and fuel encapsidated DNA synthesis.,Jacques DA, McEwan WA, Hilditch L, Price AJ, Towers GJ, James LC Nature. 2016 Aug 18;536(7616):349-53. PMID:27509857<ref>PMID:27509857</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5hgk" style="background-color:#fffaf0;"></div>

==See Also==
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human immunodeficiency virus 1]]
[[Category: Large Structures]]
[[Category: Jacques DA]]
[[Category: James LC]]
[[Category: Price AJ]]