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| | <StructureSection load='5ho4' size='340' side='right'caption='[[5ho4]], [[Resolution|resolution]] 1.85Å' scene=''> | | <StructureSection load='5ho4' size='340' side='right'caption='[[5ho4]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ho4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HO4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HO4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ho4]] is a 2 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=5HO4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HO4 FirstGlance]. <br> |
| - | </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=5ho4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ho4 OCA], [http://pdbe.org/5ho4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ho4 RCSB], [http://www.ebi.ac.uk/pdbsum/5ho4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ho4 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]] 1.85Å</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=5ho4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ho4 OCA], [https://pdbe.org/5ho4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ho4 RCSB], [https://www.ebi.ac.uk/pdbsum/5ho4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ho4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/ROA2_HUMAN ROA2_HUMAN]] Inclusion body myopathy with Paget disease of bone and frontotemporal dementia. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:23455423</ref> | + | [https://www.uniprot.org/uniprot/ROA2_HUMAN ROA2_HUMAN] Inclusion body myopathy with Paget disease of bone and frontotemporal dementia. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:23455423</ref> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ROA2_HUMAN ROA2_HUMAN]] Involved with pre-mRNA processing. Forms complexes (ribonucleosomes) with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. | + | [https://www.uniprot.org/uniprot/ROA2_HUMAN ROA2_HUMAN] Involved with pre-mRNA processing. Forms complexes (ribonucleosomes) with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Human hnRNP A2/B1 is an RNA-binding protein that plays important roles in many biological processes, including maturation, transport, and metabolism of mRNA, and gene regulation of long noncoding RNAs. hnRNP A2/B1 was reported to control the microRNAs sorting to exosomes and promote primary microRNA processing as a potential m(6)A "reader." hnRNP A2/B1 contains two RNA recognition motifs that provide sequence-specific recognition of RNA substrates. Here, we determine crystal structures of tandem RRM domains of hnRNP A2/B1 in complex with various RNA substrates, elucidating specific recognitions of AGG and UAG motifs by RRM1 and RRM2 domains, respectively. Further structural and biochemical results demonstrate multivariant binding modes for sequence-diversified RNA substrates, supporting a RNA matchmaker mechanism in hnRNP A2/B1 function. Moreover, our studies in combination with bioinformatic analysis suggest that hnRNP A2/B1 may mediate effects of m(6)A through a "m(6)A switch" mechanism, instead of acting as a direct "reader" of m(6)A modification.
| + | |
| - | | + | |
| - | Molecular basis for the specific and multivariant recognitions of RNA substrates by human hnRNP A2/B1.,Wu B, Su S, Patil DP, Liu H, Gan J, Jaffrey SR, Ma J Nat Commun. 2018 Jan 29;9(1):420. doi: 10.1038/s41467-017-02770-z. PMID:29379020<ref>PMID:29379020</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5ho4" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gan, J H]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Ma, J B]] | + | [[Category: Gan JH]] |
| - | [[Category: Su, S C]] | + | [[Category: Ma JB]] |
| - | [[Category: Wu, B X]] | + | [[Category: Su SC]] |
| - | [[Category: Hnrnpa2b1]] | + | [[Category: Wu BX]] |
| - | [[Category: Rna binding protein-rna complex]]
| + | |
| - | [[Category: Rrm]]
| + | |
| Structural highlights
Disease
ROA2_HUMAN Inclusion body myopathy with Paget disease of bone and frontotemporal dementia. The disease is caused by mutations affecting the gene represented in this entry.[1]
Function
ROA2_HUMAN Involved with pre-mRNA processing. Forms complexes (ribonucleosomes) with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus.
References
- ↑ Kim HJ, Kim NC, Wang YD, Scarborough EA, Moore J, Diaz Z, MacLea KS, Freibaum B, Li S, Molliex A, Kanagaraj AP, Carter R, Boylan KB, Wojtas AM, Rademakers R, Pinkus JL, Greenberg SA, Trojanowski JQ, Traynor BJ, Smith BN, Topp S, Gkazi AS, Miller J, Shaw CE, Kottlors M, Kirschner J, Pestronk A, Li YR, Ford AF, Gitler AD, Benatar M, King OD, Kimonis VE, Ross ED, Weihl CC, Shorter J, Taylor JP. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Nature. 2013 Mar 28;495(7442):467-73. doi: 10.1038/nature11922. Epub 2013 Mar 3. PMID:23455423 doi:http://dx.doi.org/10.1038/nature11922
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