4rwp - Revision history

OCA at 12:56, 1 March 2024

OCA — Fri, 01 Mar 2024 12:56:17 GMT

←Older revision		Revision as of 12:56, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== 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>		<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='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>	+	</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>		</table>
	== Function ==		== 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>		[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>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	2'-5'-Oligoadenylate synthetases (OASs) produce the second messenger 2'-5'-oligoadenylate, which activates RNase L to induce an intrinsic antiviral state. We report on the crystal structures of catalytic intermediates of OAS1 including the OAS1.dsRNA complex without substrates, with a donor substrate, and with both donor and acceptor substrates. Combined with kinetic studies of point mutants and the previously published structure of the apo form of OAS1, the new data suggest a sequential mechanism of OAS activation and show the individual roles of each component. They reveal a dsRNA-mediated push-pull effect responsible for large conformational changes in OAS1, the catalytic role of the active site Mg(2+), and the structural basis for the 2'-specificity of product formation. Our data reveal similarities and differences in the activation mechanisms of members of the OAS/cyclic GMP-AMP synthase family of innate immune sensors. In particular, they show how helix 3103-alpha5 blocks the synthesis of cyclic dinucleotides by OAS1.
-
-	The Activation Mechanism of 2'-5'-Oligoadenylate Synthetase Gives New Insights Into OAS/cGAS Triggers of Innate Immunity.,Lohofener J, Steinke N, Kay-Fedorov P, Baruch P, Nikulin A, Tishchenko S, Manstein DJ, Fedorov R Structure. 2015 May 5;23(5):851-62. doi: 10.1016/j.str.2015.03.012. Epub 2015 Apr, 16. PMID:25892109<ref>PMID:25892109</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4rwp" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:31, 8 March 2023

OCA — Wed, 08 Mar 2023 08:31:53 GMT

←Older revision		Revision as of 08:31, 8 March 2023
Line 3:		Line 3:
	<StructureSection load='4rwp' size='340' side='right'caption='[[4rwp]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='4rwp' size='340' side='right'caption='[[4rwp]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4rwp]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Pig Pig~~]. 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 [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4RWP FirstGlance]. <br>	+	<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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4rwn\|4rwn]], [[4rwo\|4rwo]], [[4rwq\|4rwq]]</td></tr>~~	+	</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>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">OAS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG])</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2'-5'_oligoadenylate_synthase 2'-5' oligoadenylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.84 2.7.7.84] </span></td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4rwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rwp OCA], [~~http~~://pdbe.org/4rwp PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4rwp RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4rwp PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4rwp ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://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>	+	[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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 21:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: 2'-5' oligoadenylate synthase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Pig~~]]	+	[[Category: Sus scrofa]]
-	[[Category: Baruch, P]]	+	[[Category: Synthetic construct]]
-	[[Category: Fedorov, R]]	+	[[Category: Baruch P]]
-	[[Category: Kay-Fedorov, P]]	+	[[Category: Fedorov R]]
-	[[Category: Lohoefener, J]]	+	[[Category: Kay-Fedorov P]]
-	[[Category: Manstein~~, D J~~]]	+	[[Category: Lohoefener J]]
-	[[Category: Nikulin, A]]	+	[[Category: Manstein DJ]]
-	[[Category: Steinke, N]]	+	[[Category: Nikulin A]]
-	[[Category: Tishchenko, S]]	+	[[Category: Steinke N]]
-	~~[[Category: Dsrna-activated]]~~	+	[[Category: Tishchenko S]]
-	~~[[Category: Interferon-induced]]~~	+
-	~~[[Category: Transferase-rna complex~~]]	+

OCA at 10:02, 1 May 2019

OCA — Wed, 01 May 2019 10:02:42 GMT

←Older revision		Revision as of 10:02, 1 May 2019
Line 1:		Line 1:

	==Crystal structure of porcine OAS1 in complex with dsRNA==		==Crystal structure of porcine OAS1 in complex with dsRNA==
-	<StructureSection load='4rwp' size='340' side='right' caption='[[4rwp]], [[Resolution\|resolution]] 2.25Å' scene=''>	+	<StructureSection load='4rwp' size='340' side='right'caption='[[4rwp]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4rwp]] is a 3 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RWP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4rwp]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RWP FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4rwn\|4rwn]], [[4rwo\|4rwo]], [[4rwq\|4rwq]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4rwn\|4rwn]], [[4rwo\|4rwo]], [[4rwq\|4rwq]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">OAS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2'-5'_oligoadenylate_synthase 2'-5' oligoadenylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.84 2.7.7.84] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2'-5'_oligoadenylate_synthase 2'-5' oligoadenylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.84 2.7.7.84] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4rwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rwp OCA], [http://pdbe.org/4rwp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rwp RCSB], [http://www.ebi.ac.uk/pdbsum/4rwp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rwp ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4rwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rwp OCA], [http://pdbe.org/4rwp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rwp RCSB], [http://www.ebi.ac.uk/pdbsum/4rwp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rwp ProSAT]</span></td></tr>
Line 24:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: 2'-5' oligoadenylate synthase]]		[[Category: 2'-5' oligoadenylate synthase]]
		+	[[Category: Large Structures]]
		+	[[Category: Pig]]
	[[Category: Baruch, P]]		[[Category: Baruch, P]]
	[[Category: Fedorov, R]]		[[Category: Fedorov, R]]

OCA at 01:58, 10 March 2017

OCA — Fri, 10 Mar 2017 01:58:13 GMT

←Older revision		Revision as of 01:58, 10 March 2017
Line 1:		Line 1:
		+
	==Crystal structure of porcine OAS1 in complex with dsRNA==		==Crystal structure of porcine OAS1 in complex with dsRNA==
	<StructureSection load='4rwp' size='340' side='right' caption='[[4rwp]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='4rwp' size='340' side='right' caption='[[4rwp]], [[Resolution\|resolution]] 2.25Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4rwn\|4rwn]], [[4rwo\|4rwo]], [[4rwq\|4rwq]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4rwn\|4rwn]], [[4rwo\|4rwo]], [[4rwq\|4rwq]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2'-5'_oligoadenylate_synthase 2'-5' oligoadenylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.84 2.7.7.84] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2'-5'_oligoadenylate_synthase 2'-5' oligoadenylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.84 2.7.7.84] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4rwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rwp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rwp RCSB], [http://www.ebi.ac.uk/pdbsum/4rwp PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4rwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rwp OCA], [http://pdbe.org/4rwp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rwp RCSB], [http://www.ebi.ac.uk/pdbsum/4rwp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rwp ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4rwp" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:10, 20 May 2015

OCA — Wed, 20 May 2015 12:10:39 GMT

←Older revision		Revision as of 12:10, 20 May 2015
Line 1:		Line 1:
-	'''~~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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RWP FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4rwn\|4rwn]], [[4rwo\|4rwo]], [[4rwq\|4rwq]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2'-5'_oligoadenylate_synthase 2'-5' oligoadenylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.84 2.7.7.84] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4rwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rwp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rwp RCSB], [http://www.ebi.ac.uk/pdbsum/4rwp PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	2'-5'-Oligoadenylate synthetases (OASs) produce the second messenger 2'-5'-oligoadenylate, which activates RNase L to induce an intrinsic antiviral state. We report on the crystal structures of catalytic intermediates of OAS1 including the OAS1.dsRNA complex without substrates, with a donor substrate, and with both donor and acceptor substrates. Combined with kinetic studies of point mutants and the previously published structure of the apo form of OAS1, the new data suggest a sequential mechanism of OAS activation and show the individual roles of each component. They reveal a dsRNA-mediated push-pull effect responsible for large conformational changes in OAS1, the catalytic role of the active site Mg(2+), and the structural basis for the 2'-specificity of product formation. Our data reveal similarities and differences in the activation mechanisms of members of the OAS/cyclic GMP-AMP synthase family of innate immune sensors. In particular, they show how helix 3103-alpha5 blocks the synthesis of cyclic dinucleotides by OAS1.

-	The ~~entry 4rwp is ON HOLD~~	+	The Activation Mechanism of 2'-5'-Oligoadenylate Synthetase Gives New Insights Into OAS/cGAS Triggers of Innate Immunity.,Lohofener J, Steinke N, Kay-Fedorov P, Baruch P, Nikulin A, Tishchenko S, Manstein DJ, Fedorov R Structure. 2015 May 5;23(5):851-62. doi: 10.1016/j.str.2015.03.012. Epub 2015 Apr, 16. PMID:25892109<ref>PMID:25892109</ref>

-	~~Authors: Lohoefener~~, J.~~, Steinke, N~~.~~, Kay-Fedorov, P~~., Baruch, P~~., Nikulin, A., Tishchenko, S., Manstein, D.J.,~~ Fedorov, R.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~Crystal structure of porcine OAS1 in complex with dsRNA~~	+	== References ==
-	[[Category: ~~Unreleased Structures~~]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: 2'-5' oligoadenylate synthase]]
		+	[[Category: Baruch, P]]
		+	[[Category: Fedorov, R]]
		+	[[Category: Kay-Fedorov, P]]
		+	[[Category: Lohoefener, J]]
		+	[[Category: Manstein, D J]]
	[[Category: Nikulin, A]]		[[Category: Nikulin, A]]
	[[Category: Steinke, N]]		[[Category: Steinke, N]]
-	[[Category: Lohoefener, J]]
-	[[Category: Fedorov, R]]
-	[[Category: Baruch, P]]
-	[[Category: Kay-Fedorov, P]]
-	[[Category: Manstein, D.J]]
	[[Category: Tishchenko, S]]		[[Category: Tishchenko, S]]
		+	[[Category: Dsrna-activated]]
		+	[[Category: Interferon-induced]]
		+	[[Category: Transferase-rna complex]]

OCA at 17:32, 24 December 2014

OCA — Wed, 24 Dec 2014 17:32:46 GMT

←Older revision		Revision as of 17:32, 24 December 2014
Line 6:		Line 6:

	Description: Crystal structure of porcine OAS1 in complex with dsRNA		Description: Crystal structure of porcine OAS1 in complex with dsRNA
		+	[[Category: Unreleased Structures]]
		+	[[Category: Nikulin, A]]
		+	[[Category: Steinke, N]]
		+	[[Category: Lohoefener, J]]
		+	[[Category: Fedorov, R]]
		+	[[Category: Baruch, P]]
		+	[[Category: Kay-Fedorov, P]]
		+	[[Category: Manstein, D.J]]
		+	[[Category: Tishchenko, S]]

OCA: Protected "4rwp" [edit=sysop:move=sysop]

OCA — Wed, 17 Dec 2014 11:07:50 GMT

Protected "4rwp" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:07, 17 December 2014

OCA: 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...

OCA — Wed, 17 Dec 2014 11:07:48 GMT

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...

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.

Description: Crystal structure of porcine OAS1 in complex with dsRNA