View source for 5qoj


==PanDDA analysis group deposition -- Crystal Structure of DCP2 (NUDT20) in complex with FMOCR000171b==
<StructureSection load='5qoj' size='340' side='right'caption='[[5qoj]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5qoj]] 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=5QOJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5QOJ 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]] 2.05&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=JG4:2-(thiophen-2-yl)-1H-imidazole'>JG4</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=5qoj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5qoj OCA], [https://pdbe.org/5qoj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5qoj RCSB], [https://www.ebi.ac.uk/pdbsum/5qoj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5qoj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DCP2_HUMAN DCP2_HUMAN] Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs (PubMed:12417715, PubMed:12218187, PubMed:12923261, PubMed:21070968). Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP (PubMed:12486012, PubMed:12923261, PubMed:21070968). Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay (PubMed:14527413). Plays a role in replication-dependent histone mRNA degradation (PubMed:18172165). Has higher activity towards mRNAs that lack a poly(A) tail (PubMed:21070968). Has no activity towards a cap structure lacking an RNA moiety (PubMed:21070968). Blocks autophagy in nutrient-rich conditions by repressing the expression of ATG-related genes through degration of their transcripts (PubMed:26098573).<ref>PMID:12218187</ref> <ref>PMID:12417715</ref> <ref>PMID:12486012</ref> <ref>PMID:12923261</ref> <ref>PMID:14527413</ref> <ref>PMID:18172165</ref> <ref>PMID:21070968</ref> <ref>PMID:26098573</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Arrowsmith CH]]
[[Category: Bountra C]]
[[Category: Brandao-Neto J]]
[[Category: Burgess-Brown N]]
[[Category: Collins PM]]
[[Category: Douangamath A]]
[[Category: Huber K]]
[[Category: Krojer T]]
[[Category: Nelson ER]]
[[Category: Talon R]]
[[Category: Velupillai S]]
[[Category: Wang D]]
[[Category: Von Delft F]]