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9s2d
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==KHNYN exPIN nuclease== | |
| + | <StructureSection load='9s2d' size='340' side='right'caption='[[9s2d]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9s2d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9S2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9S2D 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]] 2.35Å</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=9s2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9s2d OCA], [https://pdbe.org/9s2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9s2d RCSB], [https://www.ebi.ac.uk/pdbsum/9s2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9s2d ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/KHNYN_HUMAN KHNYN_HUMAN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Zinc finger antiviral protein (ZAP) is a cytoplasmic protein central to host innate immunity to viral infection. ZAP has no intrinsic catalytic activity but inhibits viral replication by binding to CpG dinucleotides in cytoplasmic viral RNA and recruiting other factors to inhibit protein synthesis and target the RNA for degradation. KHNYN is a ZAP-binding protein required for ZAP-restriction of CpG-rich viral genomes. It contains an extended diKH, PIN nuclease, and CUElike domain, each of which are required for ZAP restriction of viral replication. Here, we report a structural, enzymological, and virological study of KHNYN's essential PIN nuclease domain. Our crystal structure reveals an extended PIN domain (ex-PIN) containing a conserved N-terminal arm region required for domain stability and an active site tetra-Asp motif, which are both required for antiviral activity. Unlike the weak activity recently reported for the PIN domain, we demonstrate that the KHNYN ex-PIN domain is a highly active Mn2+-dependent single-stranded RNA endonuclease that cleaves with a preference for ApC, ApA, and UpA dinucleotides. These observations extend our view of KHNYN antiviral activity and suggest an unforeseen role for activation by manganese ions in the ZAP-KHNYN antiviral response. | ||
| - | + | KHNYN is a manganese-dependent endoribonuclease required for ZAP-mediated antiviral restriction.,Youle RL, Lista MJ, Brudenell EL, Thompson B, Bouton C, Morris ER, Neil SJD, Swanson CM, Taylor IA Nucleic Acids Res. 2025 Nov 26;53(22):gkaf1360. doi: 10.1093/nar/gkaf1360. PMID:41404804<ref>PMID:41404804</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9s2d" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Taylor IA]] | ||
| + | [[Category: Youle RL]] | ||
Current revision
KHNYN exPIN nuclease
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