OCA at 07:02, 25 October 2023

OCA — Wed, 25 Oct 2023 07:02:40 GMT

←Older revision		Revision as of 07:02, 25 October 2023
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 7zlq is ~~ON HOLD until Paper Publication~~	+	==structure of ADAR1 dsRBD3 in complex with dsRNA==
-		+	<StructureSection load='7zlq' size='340' side='right'caption='[[7zlq]], [[Resolution\|resolution]] 2.80Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[7zlq]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=7ZLQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZLQ FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.8Å</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=7zlq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zlq OCA], [https://pdbe.org/7zlq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zlq RCSB], [https://www.ebi.ac.uk/pdbsum/7zlq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zlq ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[https://www.uniprot.org/uniprot/DSRAD_HUMAN DSRAD_HUMAN] Defects in ADAR are a cause of dyschromatosis symmetrical hereditaria (DSH) [MIM:[https://omim.org/entry/127400 127400]; also known as reticulate acropigmentation of Dohi. DSH is a pigmentary genodermatosis of autosomal dominant inheritance characterized by a mixture of hyperpigmented and hypopigmented macules distributed on the dorsal parts of the hands and feet.<ref>PMID:12916015</ref> <ref>PMID:15146470</ref> <ref>PMID:15659327</ref>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/DSRAD_HUMAN DSRAD_HUMAN] Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structure-dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Its cellular RNA substrates include: bladder cancer-associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2) and serotonin (HTR2C) and GABA receptor (GABRA3). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alters their functional activities. Exhibits low-level editing at the GRIA2 Q/R site, but edits efficiently at the R/G site and HOTSPOT1. Its viral RNA substrates include: hepatitis C virus (HCV), vesicular stomatitis virus (VSV), measles virus (MV), hepatitis delta virus (HDV), and human immunodeficiency virus type 1 (HIV-1). Exhibits either a proviral (HDV, MV, VSV and HIV-1) or an antiviral effect (HCV) and this can be editing-dependent (HDV and HCV), editing-independent (VSV and MV) or both (HIV-1). Impairs HCV replication via RNA editing at multiple sites. Enhances the replication of MV, VSV and HIV-1 through an editing-independent mechanism via suppression of EIF2AK2/PKR activation and function. Stimulates both the release and infectivity of HIV-1 viral particles by an editing-dependent mechanism where it associates with viral RNAs and edits adenosines in the 5'UTR and the Rev and Tat coding sequence. Can enhance viral replication of HDV via A-to-I editing at a site designated as amber/W, thereby changing an UAG amber stop codon to an UIG tryptophan (W) codon that permits synthesis of the large delta antigen (L-HDAg) which has a key role in the assembly of viral particles. However, high levels of ADAR1 inhibit HDV replication.<ref>PMID:15556947</ref> <ref>PMID:15858013</ref> <ref>PMID:16475990</ref> <ref>PMID:17079286</ref> <ref>PMID:19710021</ref> <ref>PMID:19605474</ref> <ref>PMID:19651874</ref> <ref>PMID:19908260</ref> <ref>PMID:21289159</ref> <ref>PMID:22278222</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Homo sapiens]]
		+	[[Category: Large Structures]]
		+	[[Category: Synthetic construct]]
		+	[[Category: Barraud P]]
		+	[[Category: Mboukou A]]

OCA at 04:04, 13 July 2022

OCA — Wed, 13 Jul 2022 04:04:28 GMT

←Older revision		Revision as of 04:04, 13 July 2022
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 7zlq is ON HOLD	+	The entry 7zlq is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "7zlq" [edit=sysop:move=sysop]

OCA — Wed, 27 Apr 2022 10:40:29 GMT

Protected "7zlq" [edit=sysop:move=sysop]

←Older revision

Revision as of 10:40, 27 April 2022

OCA: New page: '''Unreleased structure''' The entry 7zlq is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 27 Apr 2022 10:40:28 GMT

New page: '''Unreleased structure''' The entry 7zlq is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 7zlq is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]

7zlq - Revision history

OCA at 07:02, 25 October 2023

OCA at 04:04, 13 July 2022

OCA: Protected "7zlq" [edit=sysop:move=sysop]

OCA: New page: '''Unreleased structure''' The entry 7zlq is ON HOLD Authors: Description: Category: Unreleased Structures