5wwg

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of hnRNPA2B1 in complex with AAGGACUUGC

Structural highlights

5wwg is a 2 chain structure with sequence from Homo sapiens and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.03Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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
↑ Wu B, Su S, Patil DP, Liu H, Gan J, Jaffrey SR, Ma J. Molecular basis for the specific and multivariant recognitions of RNA substrates by human hnRNP A2/B1. Nat Commun. 2018 Jan 29;9(1):420. doi: 10.1038/s41467-017-02770-z. PMID:29379020 doi:http://dx.doi.org/10.1038/s41467-017-02770-z

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5wwg"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5wwg is ON HOLD
+==Crystal structure of hnRNPA2B1 in complex with AAGGACUUGC==
+<StructureSection load='5wwg' size='340' side='right'caption='[[5wwg]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5wwg]] 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=5WWG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WWG FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.03&#8491;</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=5wwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wwg OCA], [https://pdbe.org/5wwg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wwg RCSB], [https://www.ebi.ac.uk/pdbsum/5wwg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wwg ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[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 ==
+[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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5wwg" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Synthetic construct]]
+[[Category: Ma JB]]
+[[Category: Su SC]]
+[[Category: Wu BX]]

5wwg

From Proteopedia

Current revision

Crystal structure of hnRNPA2B1 in complex with AAGGACUUGC

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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