5zi6 - Revision history

OCA at 10:27, 27 March 2024

OCA — Wed, 27 Mar 2024 10:27:55 GMT

←Older revision		Revision as of 10:27, 27 March 2024
Line 1:		Line 1:

	==The RING domain structure of MEX-3C==		==The RING domain structure of MEX-3C==
-	<StructureSection load='5zi6' size='340' side='right' caption='[[5zi6]], [[Resolution\|resolution]] 2.20Å' scene=''>	+	<StructureSection load='5zi6' size='340' side='right'caption='[[5zi6]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5zi6]] is a 8 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZI6 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5ZI6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5zi6]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZI6 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.2Å</td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~">~~<b>~~[[~~Gene~~\|~~Gene:~~]]~~</b></td><td class="sblockDat">MEX3C ([http://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=9606 HUMAN])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks~~'>~~[http://en.wikipedia.org/wiki/RING-type_E3_ubiquitin_transferase RING-type E3 ubiquitin transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.27 2.3.2.27]~~ </~~span~~></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=5zi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zi6 OCA], [https://pdbe.org/5zi6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zi6 RCSB], [https://www.ebi.ac.uk/pdbsum/5zi6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zi6 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=5zi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zi6 OCA], [~~http~~://pdbe.org/5zi6 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5zi6 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5zi6 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5zi6 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/MEX3C_HUMAN MEX3C_HUMAN]] Genetic variations in MEX3C may be associated with susceptibility to essential hypertension.<ref>PMID:17015768</ref>	+	[https://www.uniprot.org/uniprot/MEX3C_HUMAN MEX3C_HUMAN] Genetic variations in MEX3C may be associated with susceptibility to essential hypertension.<ref>PMID:17015768</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/MEX3C_HUMAN MEX3C_HUMAN]] E3 ubiquitin ligase responsible for the post-transcriptional regulation of common HLA-A allotypes. Binds to the 3' UTR of HLA-A2 mRNA, and regulates its levels by promoting mRNA decay. RNA binding is sufficient to prevent translation, but ubiquitin ligase activity is required for mRNA degradation.<ref>PMID:22863774</ref> <ref>PMID:23446422</ref>	+	[https://www.uniprot.org/uniprot/MEX3C_HUMAN MEX3C_HUMAN] E3 ubiquitin ligase responsible for the post-transcriptional regulation of common HLA-A allotypes. Binds to the 3' UTR of HLA-A2 mRNA, and regulates its levels by promoting mRNA decay. RNA binding is sufficient to prevent translation, but ubiquitin ligase activity is required for mRNA degradation.<ref>PMID:22863774</ref> <ref>PMID:23446422</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	MEX-3C, a novel RNA binding E3 ubiquitin ligases, contains two N-terminal heterogeneous nuclear ribonucleoprotein K homology (KH) domains and C-terminal Ring finger domain. Recent evidence has suggested that human MEX-3C has a strong bondage with carcinogenesis and the MEX-3C-mediated ubiquitination of RIG-I is essential for the antiviral innate immune response. Moreover, the Ring finger domain of MEX-3C could regulate the degradation of HLA-A2 (an MHC-I allotype) mRNA with a novel mechanism. However, the structural basis for the ubiquitination catalyzed by hMEX-3C Ring finger domain remains evasive. In this study, we solved the crystal structure of dimeric Ring finger domain of hMEX-3C and compared it with the complex structure of MDM2/MDMX-UbcH5b-Ub. Our ubiquitination assay demonstrated that the Ring finger domain of hMEX-3C acts as a ubiquitin E3 ligase in vitro, cooperating with specific E2 to mediate ubiquitination. Then, we identified several key residues in Ring finger domain of hMEX-3C possibly involved in the interaction with E2-Ub conjugate and analyzed the E3 ligase activities of wild type and mutants at key sites. Additionally, zinc chelation experiments indicated that the intact structural stability is essential for the self-ubiquitination activity of the Ring finger domain of hMEX-3C. Taken together, our studies provided new insight into the mechanism of the Ring finger domain of hMEX-3C that may play an important role in eliciting antiviral immune responses and therapeutic interventions.	+

-	Structural and functional characterization of hMEX-3C Ring finger domain as an E3 ubiquitin ligase.,Moududee SA, Jiang Y, Gilbert N, Xie G, Xu Z, Wu J, Gong Q, Tang Y, Shi Y Protein Sci. 2018 Sep;27(9):1661-1669. doi: 10.1002/pro.3473. PMID:30095198<ref>PMID:30095198</ref>	+	==See Also==
-		+	*[[Ubiquitin protein ligase 3D structures\|Ubiquitin protein ligase 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class~~=~~"pdbe-citations 5zi6" style~~=~~"background-color:#fffaf0;"></div>~~	+
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~RING-type E3 ubiquitin transferase~~]]	+	[[Category: Large Structures]]
-	[[Category: Moududee~~, S A~~]]	+	[[Category: Moududee SA]]
-	[[Category: Tang, Y]]	+	[[Category: Tang Y]]
-	~~[[Category: E3 liagase]]~~	+
-	~~[[Category: Ligase]]~~	+
-	~~[[Category: Mex-3c]]~~	+
-	~~[[Category: Ring domain]]~~	+
-	~~[[Category: Ubiquitination~~]]	+

OCA at 12:35, 7 November 2018

OCA — Wed, 07 Nov 2018 12:35:44 GMT

←Older revision		Revision as of 12:35, 7 November 2018
Line 3:		Line 3:
	<StructureSection load='5zi6' size='340' side='right' caption='[[5zi6]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='5zi6' size='340' side='right' caption='[[5zi6]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5zi6]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZI6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZI6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5zi6]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZI6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZI6 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MEX3C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RING-type_E3_ubiquitin_transferase RING-type E3 ubiquitin transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.27 2.3.2.27] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RING-type_E3_ubiquitin_transferase RING-type E3 ubiquitin transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.27 2.3.2.27] </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=5zi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zi6 OCA], [http://pdbe.org/5zi6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zi6 RCSB], [http://www.ebi.ac.uk/pdbsum/5zi6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zi6 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=5zi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zi6 OCA], [http://pdbe.org/5zi6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zi6 RCSB], [http://www.ebi.ac.uk/pdbsum/5zi6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zi6 ProSAT]</span></td></tr>
Line 25:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: RING-type E3 ubiquitin transferase]]		[[Category: RING-type E3 ubiquitin transferase]]
	[[Category: Moududee, S A]]		[[Category: Moududee, S A]]

OCA at 05:47, 24 October 2018

OCA — Wed, 24 Oct 2018 05:47:50 GMT

←Older revision		Revision as of 05:47, 24 October 2018
Line 1:		Line 1:
-	'''Unreleased structure'''

-	The ~~entry~~ 5zi6 is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==The RING domain structure of MEX-3C==
		+	<StructureSection load='5zi6' size='340' side='right' caption='[[5zi6]], [[Resolution\|resolution]] 2.20Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5zi6]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZI6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZI6 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RING-type_E3_ubiquitin_transferase RING-type E3 ubiquitin transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.27 2.3.2.27] </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=5zi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zi6 OCA], [http://pdbe.org/5zi6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zi6 RCSB], [http://www.ebi.ac.uk/pdbsum/5zi6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zi6 ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/MEX3C_HUMAN MEX3C_HUMAN]] Genetic variations in MEX3C may be associated with susceptibility to essential hypertension.<ref>PMID:17015768</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/MEX3C_HUMAN MEX3C_HUMAN]] E3 ubiquitin ligase responsible for the post-transcriptional regulation of common HLA-A allotypes. Binds to the 3' UTR of HLA-A2 mRNA, and regulates its levels by promoting mRNA decay. RNA binding is sufficient to prevent translation, but ubiquitin ligase activity is required for mRNA degradation.<ref>PMID:22863774</ref> <ref>PMID:23446422</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	MEX-3C, a novel RNA binding E3 ubiquitin ligases, contains two N-terminal heterogeneous nuclear ribonucleoprotein K homology (KH) domains and C-terminal Ring finger domain. Recent evidence has suggested that human MEX-3C has a strong bondage with carcinogenesis and the MEX-3C-mediated ubiquitination of RIG-I is essential for the antiviral innate immune response. Moreover, the Ring finger domain of MEX-3C could regulate the degradation of HLA-A2 (an MHC-I allotype) mRNA with a novel mechanism. However, the structural basis for the ubiquitination catalyzed by hMEX-3C Ring finger domain remains evasive. In this study, we solved the crystal structure of dimeric Ring finger domain of hMEX-3C and compared it with the complex structure of MDM2/MDMX-UbcH5b-Ub. Our ubiquitination assay demonstrated that the Ring finger domain of hMEX-3C acts as a ubiquitin E3 ligase in vitro, cooperating with specific E2 to mediate ubiquitination. Then, we identified several key residues in Ring finger domain of hMEX-3C possibly involved in the interaction with E2-Ub conjugate and analyzed the E3 ligase activities of wild type and mutants at key sites. Additionally, zinc chelation experiments indicated that the intact structural stability is essential for the self-ubiquitination activity of the Ring finger domain of hMEX-3C. Taken together, our studies provided new insight into the mechanism of the Ring finger domain of hMEX-3C that may play an important role in eliciting antiviral immune responses and therapeutic interventions.

-	~~Authors:~~ Moududee, ~~S.A.~~, Tang, Y.	+	Structural and functional characterization of hMEX-3C Ring finger domain as an E3 ubiquitin ligase.,Moududee SA, Jiang Y, Gilbert N, Xie G, Xu Z, Wu J, Gong Q, Tang Y, Shi Y Protein Sci. 2018 Sep;27(9):1661-1669. doi: 10.1002/pro.3473. PMID:30095198<ref>PMID:30095198</ref>

-	~~Description~~: ~~The~~ RING ~~domain structure of MEX~~-3C	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5zi6" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: RING-type E3 ubiquitin transferase]]
		+	[[Category: Moududee, S A]]
	[[Category: Tang, Y]]		[[Category: Tang, Y]]
-	[[Category: ~~Moududee, S.A~~]]	+	[[Category: E3 liagase]]
		+	[[Category: Ligase]]
		+	[[Category: Mex-3c]]
		+	[[Category: Ring domain]]
		+	[[Category: Ubiquitination]]

OCA at 05:09, 28 March 2018

OCA — Wed, 28 Mar 2018 05:09:04 GMT

←Older revision		Revision as of 05:09, 28 March 2018
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5zi6 is ON HOLD	+	The entry 5zi6 is ON HOLD until Paper Publication

	Authors: Moududee, S.A., Tang, Y.		Authors: Moududee, S.A., Tang, Y.

OCA: Protected "5zi6" [edit=sysop:move=sysop]

OCA — Wed, 21 Mar 2018 06:02:33 GMT

Protected "5zi6" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:02, 21 March 2018

OCA: New page: '''Unreleased structure''' The entry 5zi6 is ON HOLD Authors: Moududee, S.A., Tang, Y. Description: The RING domain structure of MEX-3C Category: Unreleased Structures [[Category: ...

OCA — Wed, 21 Mar 2018 06:02:31 GMT

New page: '''Unreleased structure''' The entry 5zi6 is ON HOLD Authors: Moududee, S.A., Tang, Y. Description: The RING domain structure of MEX-3C Category: Unreleased Structures [[Category: ...

New page

'''Unreleased structure'''

The entry 5zi6 is ON HOLD

Authors: Moududee, S.A., Tang, Y.

Description: The RING domain structure of MEX-3C
[[Category: Unreleased Structures]]
[[Category: Tang, Y]]
[[Category: Moududee, S.A]]