6brg: Difference between revisions

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<StructureSection load='6brg' size='340' side='right'caption='[[6brg]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
<StructureSection load='6brg' size='340' side='right'caption='[[6brg]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6brg]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BRG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6BRG FirstGlance]. <br>
<table><tr><td colspan='2'>[[6brg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BRG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BRG FirstGlance]. <br>
</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6brg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6brg OCA], [http://pdbe.org/6brg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6brg RCSB], [http://www.ebi.ac.uk/pdbsum/6brg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6brg ProSAT]</span></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6brg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6brg OCA], [https://pdbe.org/6brg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6brg RCSB], [https://www.ebi.ac.uk/pdbsum/6brg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6brg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SAMH1_MOUSE SAMH1_MOUSE] Protein that acts both as a host restriction factor involved in defense response to virus and as a regulator of DNA end resection at stalled replication forks (By similarity). Has deoxynucleoside triphosphate (dNTPase) activity, which is required to restrict infection by viruses: dNTPase activity reduces cellular dNTP levels to levels too low for retroviral reverse transcription to occur, blocking early-stage virus replication in dendritic and other myeloid cells (PubMed:23972988, PubMed:23872947, PubMed:26667483, PubMed:31548683, PubMed:29379009). Likewise, suppresses LINE-1 retrotransposon activity (PubMed:26667483). In addition to virus restriction, dNTPase activity acts as a regulator of DNA precursor pools by regulating dNTP pools (By similarity). Phosphorylation at Thr-634 acts as a switch to control dNTPase-dependent and -independent functions: it inhibits dNTPase activity and ability to restrict infection by viruses, while it promotes DNA end resection at stalled replication forks (By similarity). Functions during S phase at stalled DNA replication forks to promote the resection of gapped or reversed forks: acts by stimulating the exonuclease activity of MRE11, activating the ATR-CHK1 pathway and allowing the forks to restart replication (By similarity). Its ability to promote degradation of nascent DNA at stalled replication forks is required to prevent induction of type I interferons, thereby preventing chronic inflammation (By similarity). Ability to promote DNA end resection at stalled replication forks is independent of dNTPase activity (By similarity). Enhances immunoglobulin hypermutation in B-lymphocytes by promoting transversion mutation (PubMed:29669924).[UniProtKB:Q9Y3Z3]<ref>PMID:23872947</ref> <ref>PMID:23972988</ref> <ref>PMID:26667483</ref> <ref>PMID:29379009</ref> <ref>PMID:29669924</ref> <ref>PMID:31548683</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Antonucci, J M]]
[[Category: Mus musculus]]
[[Category: Buzovetsky, O]]
[[Category: Antonucci JM]]
[[Category: Ji, X]]
[[Category: Buzovetsky O]]
[[Category: Knecht, K M]]
[[Category: Ji X]]
[[Category: Tang, C]]
[[Category: Knecht KM]]
[[Category: Wu, L]]
[[Category: Tang C]]
[[Category: Xiong, Y]]
[[Category: Wu L]]
[[Category: Allosteric regulation]]
[[Category: Xiong Y]]
[[Category: Binding site]]
[[Category: Dntpase]]
[[Category: Hydrolase]]
[[Category: Model]]
[[Category: Molecular]]
[[Category: Mouse]]
[[Category: Protein conformation]]
[[Category: Protein multimerization]]

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