|
|
| Line 3: |
Line 3: |
| | <StructureSection load='4zkf' size='340' side='right'caption='[[4zkf]], [[Resolution|resolution]] 1.82Å' scene=''> | | <StructureSection load='4zkf' size='340' side='right'caption='[[4zkf]], [[Resolution|resolution]] 1.82Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4zkf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZKF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZKF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4zkf]] is a 1 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=4ZKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZKF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDE12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4zkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zkf OCA], [https://pdbe.org/4zkf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zkf RCSB], [https://www.ebi.ac.uk/pdbsum/4zkf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zkf ProSAT]</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=4zkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zkf OCA], [http://pdbe.org/4zkf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zkf RCSB], [http://www.ebi.ac.uk/pdbsum/4zkf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zkf ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PDE12_HUMAN PDE12_HUMAN]] Enzyme that cleaves 2',5'-phosphodiester bond linking adenosines of the 5'-triphosphorylated oligoadenylates, triphosphorylated oligoadenylates referred as 2-5A modulates the 2-5A system. This enzyme degraded triphosphorylated 2-5A to produce AMP and ATP. Also cleaves 3',5'-phosphodiester bond of oligoadenylates. Plays a role as a negative regulator of the The 2-5A system that is one of the major pathways for antiviral and antitumor functions induced by interferons (IFNs). Suppression of this enzyme induces reduction of viral replication in Hela cells, thus counteracting the antiviral pathway probably by inhibiting the 2-5A system.<ref>PMID:15231837</ref> <ref>PMID:21245038</ref> <ref>PMID:21666256</ref> <ref>PMID:22285541</ref> | + | [https://www.uniprot.org/uniprot/PDE12_HUMAN PDE12_HUMAN] Enzyme that cleaves 2',5'-phosphodiester bond linking adenosines of the 5'-triphosphorylated oligoadenylates, triphosphorylated oligoadenylates referred as 2-5A modulates the 2-5A system. This enzyme degraded triphosphorylated 2-5A to produce AMP and ATP. Also cleaves 3',5'-phosphodiester bond of oligoadenylates. Plays a role as a negative regulator of the The 2-5A system that is one of the major pathways for antiviral and antitumor functions induced by interferons (IFNs). Suppression of this enzyme induces reduction of viral replication in Hela cells, thus counteracting the antiviral pathway probably by inhibiting the 2-5A system.<ref>PMID:15231837</ref> <ref>PMID:21245038</ref> <ref>PMID:21666256</ref> <ref>PMID:22285541</ref> |
| | | | |
| | ==See Also== | | ==See Also== |
| Line 17: |
Line 16: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hakoshima, T]] | + | [[Category: Hakoshima T]] |
| - | [[Category: Kim, S Y]] | + | [[Category: Kim SY]] |
| - | [[Category: Kitano, K]] | + | [[Category: Kitano K]] |
| - | [[Category: Kohno, T]] | + | [[Category: Kohno T]] |
| - | [[Category: Mori, T]] | + | [[Category: Mori T]] |
| - | [[Category: Diesterase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
PDE12_HUMAN Enzyme that cleaves 2',5'-phosphodiester bond linking adenosines of the 5'-triphosphorylated oligoadenylates, triphosphorylated oligoadenylates referred as 2-5A modulates the 2-5A system. This enzyme degraded triphosphorylated 2-5A to produce AMP and ATP. Also cleaves 3',5'-phosphodiester bond of oligoadenylates. Plays a role as a negative regulator of the The 2-5A system that is one of the major pathways for antiviral and antitumor functions induced by interferons (IFNs). Suppression of this enzyme induces reduction of viral replication in Hela cells, thus counteracting the antiviral pathway probably by inhibiting the 2-5A system.[1] [2] [3] [4]
See Also
References
- ↑ Kubota K, Nakahara K, Ohtsuka T, Yoshida S, Kawaguchi J, Fujita Y, Ozeki Y, Hara A, Yoshimura C, Furukawa H, Haruyama H, Ichikawa K, Yamashita M, Matsuoka T, Iijima Y. Identification of 2'-phosphodiesterase, which plays a role in the 2-5A system regulated by interferon. J Biol Chem. 2004 Sep 3;279(36):37832-41. Epub 2004 Jun 30. PMID:15231837 doi:http://dx.doi.org/10.1074/jbc.M400089200
- ↑ Poulsen JB, Andersen KR, Kjaer KH, Durand F, Faou P, Vestergaard AL, Talbo GH, Hoogenraad N, Brodersen DE, Justesen J, Martensen PM. Human 2'-phosphodiesterase localizes to the mitochondrial matrix with a putative function in mitochondrial RNA turnover. Nucleic Acids Res. 2011 May;39(9):3754-70. doi: 10.1093/nar/gkq1282. Epub 2011, Jan 17. PMID:21245038 doi:http://dx.doi.org/10.1093/nar/gkq1282
- ↑ Rorbach J, Nicholls TJ, Minczuk M. PDE12 removes mitochondrial RNA poly(A) tails and controls translation in human mitochondria. Nucleic Acids Res. 2011 Sep 1;39(17):7750-63. doi: 10.1093/nar/gkr470. Epub 2011 , Jun 11. PMID:21666256 doi:http://dx.doi.org/10.1093/nar/gkr470
- ↑ Poulsen JB, Andersen KR, Kjaer KH, Vestergaard AL, Justesen J, Martensen PM. Characterization of human phosphodiesterase 12 and identification of a novel 2'-5' oligoadenylate nuclease - The ectonucleotide pyrophosphatase/phosphodiesterase 1. Biochimie. 2012 May;94(5):1098-107. doi: 10.1016/j.biochi.2012.01.012. Epub 2012 , Jan 24. PMID:22285541 doi:http://dx.doi.org/10.1016/j.biochi.2012.01.012
|
