4rwq: Difference between revisions

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'''Unreleased structure'''


The entry 4rwq is ON HOLD  until Paper Publication
==Crystal structure of the apo-state of porcine OAS1==
 
<StructureSection load='4rwq' size='340' side='right'caption='[[4rwq]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
Authors: Lohoefener, J., Steinke, N., Kay-Fedorov, P., Baruch, P., Nikulin, A., Tishchenko, S., Manstein, D.J., Fedorov, R.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[4rwq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RWQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RWQ FirstGlance]. <br>
Description: Crystal structure of the apo-state of porcine OAS1
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
[[Category: Unreleased Structures]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4rwq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rwq OCA], [https://pdbe.org/4rwq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rwq RCSB], [https://www.ebi.ac.uk/pdbsum/4rwq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rwq ProSAT]</span></td></tr>
[[Category: Nikulin, A]]
</table>
[[Category: Steinke, N]]
== Function ==
[[Category: Lohoefener, J]]
[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>
[[Category: Fedorov, R]]
== References ==
[[Category: Baruch, P]]
<references/>
[[Category: Kay-Fedorov, P]]
__TOC__
[[Category: Manstein, D.J]]
</StructureSection>
[[Category: Tishchenko, S]]
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[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]]
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