4rwp
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4rwp is ON HOLD Authors: Lohoefener, J., Steinke, N., Kay-Fedorov, P., Baruch, P., Nikulin, A., Tishchenko, S., Manstein, D.J., Fedorov, R. Descrip...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of porcine OAS1 in complex with dsRNA== | |
| - | + | <StructureSection load='4rwp' size='340' side='right'caption='[[4rwp]], [[Resolution|resolution]] 2.25Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4rwp]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RWP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RWP 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]] 2.25Å</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=4rwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rwp OCA], [https://pdbe.org/4rwp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rwp RCSB], [https://www.ebi.ac.uk/pdbsum/4rwp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rwp ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/OAS1_PIG OAS1_PIG] Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. The secreted form displays antiviral effect against vesicular stomatitis virus (VSV), herpes simplex virus type 2 (HSV-2), and encephalomyocarditis virus (EMCV) and stimulates the alternative antiviral pathway independent of RNase L.<ref>PMID:20844035</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Sus scrofa]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Baruch P]] | ||
| + | [[Category: Fedorov R]] | ||
| + | [[Category: Kay-Fedorov P]] | ||
| + | [[Category: Lohoefener J]] | ||
| + | [[Category: Manstein DJ]] | ||
| + | [[Category: Nikulin A]] | ||
| + | [[Category: Steinke N]] | ||
| + | [[Category: Tishchenko S]] | ||
Current revision
Crystal structure of porcine OAS1 in complex with dsRNA
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