5wwe

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==Crystal structure of hnRNPA2B1 in complex with RNA==
==Crystal structure of hnRNPA2B1 in complex with RNA==
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<StructureSection load='5wwe' size='340' side='right' caption='[[5wwe]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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<StructureSection load='5wwe' size='340' side='right'caption='[[5wwe]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5wwe]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WWE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WWE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5wwe]] 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=5WWE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WWE FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5wwf|5wwf]], [[5wwg|5wwg]], [[5wwh|5wwh]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<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=5wwe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wwe OCA], [http://pdbe.org/5wwe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wwe RCSB], [http://www.ebi.ac.uk/pdbsum/5wwe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wwe ProSAT]</span></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=5wwe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wwe OCA], [https://pdbe.org/5wwe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wwe RCSB], [https://www.ebi.ac.uk/pdbsum/5wwe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wwe ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[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>
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[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 ==
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[[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.
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[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5wwe" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ma, J B]]
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[[Category: Homo sapiens]]
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[[Category: Su, S C]]
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[[Category: Large Structures]]
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[[Category: Wu, B X]]
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[[Category: Synthetic construct]]
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[[Category: Hnrnp]]
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[[Category: Ma JB]]
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[[Category: Rna binding protein-rna complex]]
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[[Category: Su SC]]
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[[Category: Rrm]]
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[[Category: Wu BX]]

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Crystal structure of hnRNPA2B1 in complex with RNA

PDB ID 5wwe

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