3u9g

From Proteopedia

(Difference between revisions)

Revision as of 15:35, 5 August 2016

Crystal structure of the Zinc finger antiviral protein

Structural highlights

3u9g is a 1 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	Zc3hav1, Zap (Buffalo rat)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

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^[8]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gao G, Guo X, Goff SP. Inhibition of retroviral RNA production by ZAP, a CCCH-type zinc finger protein. Science. 2002 Sep 6;297(5587):1703-6. PMID:12215647 doi:http://dx.doi.org/10.1126/science.1074276
↑ Bick MJ, Carroll JW, Gao G, Goff SP, Rice CM, MacDonald MR. Expression of the zinc-finger antiviral protein inhibits alphavirus replication. J Virol. 2003 Nov;77(21):11555-62. PMID:14557641
↑ Muller S, Moller P, Bick MJ, Wurr S, Becker S, Gunther S, Kummerer BM. Inhibition of filovirus replication by the zinc finger antiviral protein. J Virol. 2007 Mar;81(5):2391-400. Epub 2006 Dec 20. PMID:17182693 doi:http://dx.doi.org/10.1128/JVI.01601-06
↑ Guo X, Ma J, Sun J, Gao G. The zinc-finger antiviral protein recruits the RNA processing exosome to degrade the target mRNA. Proc Natl Acad Sci U S A. 2007 Jan 2;104(1):151-6. Epub 2006 Dec 21. PMID:17185417 doi:http://dx.doi.org/10.1073/pnas.0607063104
↑ MacDonald MR, Machlin ES, Albin OR, Levy DE. The zinc finger antiviral protein acts synergistically with an interferon-induced factor for maximal activity against alphaviruses. J Virol. 2007 Dec;81(24):13509-18. Epub 2007 Oct 10. PMID:17928353 doi:http://dx.doi.org/10.1128/JVI.00402-07
↑ Kerns JA, Emerman M, Malik HS. Positive selection and increased antiviral activity associated with the PARP-containing isoform of human zinc-finger antiviral protein. PLoS Genet. 2008 Jan;4(1):e21. doi: 10.1371/journal.pgen.0040021. PMID:18225958 doi:http://dx.doi.org/10.1371/journal.pgen.0040021
↑ Zhu Y, Chen G, Lv F, Wang X, Ji X, Xu Y, Sun J, Wu L, Zheng YT, Gao G. Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spliced viral mRNAs for degradation. Proc Natl Acad Sci U S A. 2011 Sep 20;108(38):15834-9. doi:, 10.1073/pnas.1101676108. Epub 2011 Aug 29. PMID:21876179 doi:http://dx.doi.org/10.1073/pnas.1101676108
↑ Chen S, Xu Y, Zhang K, Wang X, Sun J, Gao G, Liu Y. Structure of N-terminal domain of ZAP indicates how a zinc-finger protein recognizes complex RNA. Nat Struct Mol Biol. 2012 Mar 11;19(4):430-5. doi: 10.1038/nsmb.2243. PMID:22407013 doi:10.1038/nsmb.2243

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3u9g"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the Zinc finger antiviral protein==
 <StructureSection load='3u9g' size='340' side='right' caption='[[3u9g]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3u9g]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U9G FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3u9g]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U9G FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Zc3hav1, Zap ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Zc3hav1, Zap ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=3u9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u9g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u9g RCSB], [http://www.ebi.ac.uk/pdbsum/3u9g PDBsum]</span></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=3u9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u9g OCA], [http://pdbe.org/3u9g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3u9g RCSB], [http://www.ebi.ac.uk/pdbsum/3u9g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3u9g ProSAT]</span></td></tr>
 </table>
+== Function ==
+[[http://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 ==
@@ Line 15: / Line 18: @@
 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/>
 __TOC__
 </StructureSection>
-[[Category: Rattus norvegicus]]
+[[Category: Buffalo rat]]
 [[Category: Chen, S]]
 [[Category: Gao, G]]

3u9g

From Proteopedia

Revision as of 15:35, 5 August 2016

Crystal structure of the Zinc finger antiviral protein

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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