4rwn: Difference between revisions

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'''Unreleased structure'''


The entry 4rwn is ON HOLD
==Crystal structure of the pre-reactive state of porcine OAS1==
 
<StructureSection load='4rwn' size='340' side='right'caption='[[4rwn]], [[Resolution|resolution]] 2.00&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'>[[4rwn]] 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=4RWN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RWN FirstGlance]. <br>
Description: Crystal structure of the pre-reactive 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]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <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=4rwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rwn OCA], [https://pdbe.org/4rwn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rwn RCSB], [https://www.ebi.ac.uk/pdbsum/4rwn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rwn 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]]

Latest revision as of 15:56, 1 March 2024

Crystal structure of the pre-reactive state of porcine OAS1Crystal structure of the pre-reactive state of porcine OAS1

Structural highlights

4rwn is a 3 chain structure with sequence from Sus scrofa and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1]

References

  1. Kristiansen H, Scherer CA, McVean M, Iadonato SP, Vends S, Thavachelvam K, Steffensen TB, Horan KA, Kuri T, Weber F, Paludan SR, Hartmann R. Extracellular 2'-5' oligoadenylate synthetase stimulates RNase L-independent antiviral activity: a novel mechanism of virus-induced innate immunity. J Virol. 2010 Nov;84(22):11898-904. doi: 10.1128/JVI.01003-10. Epub 2010 Sep 15. PMID:20844035 doi:http://dx.doi.org/10.1128/JVI.01003-10

4rwn, resolution 2.00Å

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