3u9g: Difference between revisions

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<StructureSection load='3u9g' size='340' side='right'caption='[[3u9g]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3u9g' size='340' side='right'caption='[[3u9g]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3u9g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U9G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U9G FirstGlance]. <br>
<table><tr><td colspan='2'>[[3u9g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U9G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U9G FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.801&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Zc3hav1, Zap ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3u9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u9g OCA], [https://pdbe.org/3u9g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u9g RCSB], [https://www.ebi.ac.uk/pdbsum/3u9g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u9g ProSAT]</span></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=3u9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u9g OCA], [https://pdbe.org/3u9g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u9g RCSB], [https://www.ebi.ac.uk/pdbsum/3u9g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u9g ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ZCCHV_RAT ZCCHV_RAT]] Antiviral protein which inhibits the replication of viruses by recruiting the cellular RNA degradation machineries to degrade the viral mRNAs. Binds to a ZAP-responsive element (ZRE) present in the target viral mRNA, recruits cellular poly(A)-specific ribonuclease PARN to remove the poly(A) tail, and the 3'-5' exoribonuclease complex exosome to degrade the RNA body from the 3'-end. It also recruits the decapping complex DCP1-DCP2 through RNA helicase p72 (DDX17) to remove the cap structure of the viral mRNA to initiate its degradation from the 5'-end. Its target viruses belong to families which include retroviridae: human immunodeficiency virus type 1 (HIV-1) and moloney and murine leukemia virus (MoMLV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), togaviridae: sindbis virus (SINV) and Ross river virus (RRV). Specifically targets the multiply spliced but not unspliced or singly spliced HIV-1 mRNAs for degradation.<ref>PMID:12215647</ref> <ref>PMID:14557641</ref> <ref>PMID:17182693</ref> <ref>PMID:17185417</ref> <ref>PMID:17928353</ref> <ref>PMID:18225958</ref> <ref>PMID:21876179</ref> 
[https://www.uniprot.org/uniprot/ZCCHV_RAT ZCCHV_RAT] Antiviral protein which inhibits the replication of viruses by recruiting the cellular RNA degradation machineries to degrade the viral mRNAs. Binds to a ZAP-responsive element (ZRE) present in the target viral mRNA, recruits cellular poly(A)-specific ribonuclease PARN to remove the poly(A) tail, and the 3'-5' exoribonuclease complex exosome to degrade the RNA body from the 3'-end. It also recruits the decapping complex DCP1-DCP2 through RNA helicase p72 (DDX17) to remove the cap structure of the viral mRNA to initiate its degradation from the 5'-end. Its target viruses belong to families which include retroviridae: human immunodeficiency virus type 1 (HIV-1) and moloney and murine leukemia virus (MoMLV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), togaviridae: sindbis virus (SINV) and Ross river virus (RRV). Specifically targets the multiply spliced but not unspliced or singly spliced HIV-1 mRNAs for degradation.<ref>PMID:12215647</ref> <ref>PMID:14557641</ref> <ref>PMID:17182693</ref> <ref>PMID:17185417</ref> <ref>PMID:17928353</ref> <ref>PMID:18225958</ref> <ref>PMID:21876179</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses, such as HIV-1, by targeting viral mRNA for degradation. How ZAP recognizes its target RNA has been unclear. Here we report the crystal structure of the N-terminal domain of rat ZAP (NZAP225), the major functional domain. The overall structure of NZAP225 resembles a tractor, with four zinc-finger motifs located at the bottom. Structural and functional analyses identified multiple positively charged residues and two putative RNA-binding cavities forming a large putative RNA-binding cleft. ZAP molecules interact to form a dimer that binds to a ZAP-responsive RNA molecule containing two ZAP-binding modules. These results provide insights into how ZAP binds specifically to complex target RNA.
 
Structure of N-terminal domain of ZAP indicates how a zinc-finger protein recognizes complex RNA.,Chen S, Xu Y, Zhang K, Wang X, Sun J, Gao G, Liu Y Nat Struct Mol Biol. 2012 Mar 11;19(4):430-5. doi: 10.1038/nsmb.2243. PMID:22407013<ref>PMID:22407013</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3u9g" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Buffalo rat]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chen, S]]
[[Category: Rattus norvegicus]]
[[Category: Gao, G]]
[[Category: Chen S]]
[[Category: Liu, Y]]
[[Category: Gao G]]
[[Category: Sun, J]]
[[Category: Liu Y]]
[[Category: Wang, X]]
[[Category: Sun J]]
[[Category: Xu, Y]]
[[Category: Wang X]]
[[Category: Zhang, K]]
[[Category: Xu Y]]
[[Category: Antiviral protein]]
[[Category: Zhang K]]
[[Category: Zinc finger protein]]
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