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| | ==Structure of ADAR2 dsRBM2== | | ==Structure of ADAR2 dsRBM2== |
| - | <StructureSection load='2b7v' size='340' side='right'caption='[[2b7v]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2b7v' size='340' side='right'caption='[[2b7v]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2b7v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B7V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B7V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2b7v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B7V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B7V FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2b7t|2b7t]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Adarb1, Red1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2b7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b7v OCA], [https://pdbe.org/2b7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b7v RCSB], [https://www.ebi.ac.uk/pdbsum/2b7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b7v ProSAT]</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=2b7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b7v OCA], [https://pdbe.org/2b7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b7v RCSB], [https://www.ebi.ac.uk/pdbsum/2b7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b7v ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RED1_RAT RED1_RAT]] 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 GRIK2) and serotonin (HTR2C), GABA receptor (GABRA3) and potassium voltage-gated channel (KCNA1). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alter their functional activities. Edits GRIA2 at both the Q/R and R/G sites efficiently but converts the adenosine in hotspot1 much less efficiently (By similarity). Can inhibit cell proliferation and migration and can stimulate exocytosis.<ref>PMID:20501795</ref> <ref>PMID:16472753</ref> <ref>PMID:20946981</ref>
| + | [https://www.uniprot.org/uniprot/RED1_RAT RED1_RAT] 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 GRIK2) and serotonin (HTR2C), GABA receptor (GABRA3) and potassium voltage-gated channel (KCNA1). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alter their functional activities. Edits GRIA2 at both the Q/R and R/G sites efficiently but converts the adenosine in hotspot1 much less efficiently (By similarity). Can inhibit cell proliferation and migration and can stimulate exocytosis.<ref>PMID:20501795</ref> <ref>PMID:16472753</ref> <ref>PMID:20946981</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Allain, F H.T]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Emeson, R B]] | + | [[Category: Allain FH-T]] |
| - | [[Category: Skrisovska, L]] | + | [[Category: Emeson RB]] |
| - | [[Category: Stefl, R]] | + | [[Category: Skrisovska L]] |
| - | [[Category: Xu, M]] | + | [[Category: Stefl R]] |
| - | [[Category: Hydrolase]]
| + | [[Category: Xu M]] |
| - | [[Category: Rna editing]]
| + | |
| - | [[Category: Rna-binding protein]]
| + | |
| Structural highlights
Function
RED1_RAT 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 GRIK2) and serotonin (HTR2C), GABA receptor (GABRA3) and potassium voltage-gated channel (KCNA1). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alter their functional activities. Edits GRIA2 at both the Q/R and R/G sites efficiently but converts the adenosine in hotspot1 much less efficiently (By similarity). Can inhibit cell proliferation and migration and can stimulate exocytosis.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Adenosine deaminases that act on RNA (ADARs) site-selectively modify adenosines to inosines within RNA transcripts, thereby recoding genomic information. How ADARs select specific adenosine moieties for deamination is poorly understood. Here, we report NMR structures of the two double-stranded RNA binding motifs (dsRBMs) of rat ADAR2 and an NMR chemical shift perturbation study of the interaction of the two dsRBMs with a 71 nucleotide RNA encoding the R/G site of the GluR-B. We have identified the protein and the RNA surfaces involved in complex formation, allowing us to present an NMR-based model of the complex. We have found that dsRBM1 recognizes a conserved pentaloop, whereas dsRBM2 recognizes two bulged bases adjacent to the editing site, demonstrating RNA structure-dependent recognition by the ADAR2 dsRBMs. In vitro mutagenesis studies with both the protein and the RNA further support our structural findings.
Structure and specific RNA binding of ADAR2 double-stranded RNA binding motifs.,Stefl R, Xu M, Skrisovska L, Emeson RB, Allain FH Structure. 2006 Feb;14(2):345-55. PMID:16472753[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yang L, Zhao L, Gan Z, He Z, Xu J, Gao X, Wang X, Han W, Chen L, Xu T, Li W, Liu Y. Deficiency in RNA editing enzyme ADAR2 impairs regulated exocytosis. FASEB J. 2010 Oct;24(10):3720-32. doi: 10.1096/fj.09-152363. Epub 2010 May 25. PMID:20501795 doi:http://dx.doi.org/10.1096/fj.09-152363
- ↑ Stefl R, Xu M, Skrisovska L, Emeson RB, Allain FH. Structure and specific RNA binding of ADAR2 double-stranded RNA binding motifs. Structure. 2006 Feb;14(2):345-55. PMID:16472753 doi:10.1016/j.str.2005.11.013
- ↑ Stefl R, Oberstrass FC, Hood JL, Jourdan M, Zimmermann M, Skrisovska L, Maris C, Peng L, Hofr C, Emeson RB, Allain FH. The solution structure of the ADAR2 dsRBM-RNA complex reveals a sequence-specific readout of the minor groove. Cell. 2010 Oct 15;143(2):225-37. PMID:20946981 doi:10.1016/j.cell.2010.09.026
- ↑ Stefl R, Xu M, Skrisovska L, Emeson RB, Allain FH. Structure and specific RNA binding of ADAR2 double-stranded RNA binding motifs. Structure. 2006 Feb;14(2):345-55. PMID:16472753 doi:10.1016/j.str.2005.11.013
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