7wm3: Difference between revisions

Revision as of 07:48, 11 January 2023

hnRNP A2/B1 RRMs in complex with single-stranded DNA

Structural highlights

7wm3 is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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

Heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP A2/B1) has been identified as a nuclear DNA sensor. Upon viral infection, hnRNP A2/B1 recognizes pathogen-derived DNA as a homodimer, which is a prerequisite for its translocation to the cytoplasm to activate the interferon response. However, the DNA binding mechanism inducing hnRNP A2/B1 homodimerization is unknown. Here, we show the crystal structure of the RNA recognition motif (RRM) of hnRNP A2/B1 in complex with a U-shaped ssDNA, which mediates the formation of a newly observed protein dimer. Our biochemical assays and mutagenesis studies confirm that the hnRNP A2/B1 homodimer forms in solution by binding to pre-generated ssDNA or dsDNA with a U-shaped bulge. These results depict a potential functional state of hnRNP A2/B1 in antiviral immunity and other cellular processes.

Structural Insight Into hnRNP A2/B1 Homodimerization and DNA Recognition.,Liu Y, Abula A, Xiao H, Guo H, Li T, Zheng L, Chen B, Nguyen HC, Ji X J Mol Biol. 2022 Dec 14;435(3):167920. doi: 10.1016/j.jmb.2022.167920. PMID:36528084^[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:https://dx.doi.org/10.1038/nature11922
↑ Liu Y, Abula A, Xiao H, Guo H, Li T, Zheng L, Chen B, Nguyen HC, Ji X. Structural Insight Into hnRNP A2/B1 Homodimerization and DNA Recognition. J Mol Biol. 2022 Dec 14;435(3):167920. doi: 10.1016/j.jmb.2022.167920. PMID:36528084 doi:https://dx.doi.org/10.1016/j.jmb.2022.167920

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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:https://dx.doi.org/10.1038/nature11922

[2] Liu Y, Abula A, Xiao H, Guo H, Li T, Zheng L, Chen B, Nguyen HC, Ji X. Structural Insight Into hnRNP A2/B1 Homodimerization and DNA Recognition. J Mol Biol. 2022 Dec 14;435(3):167920. doi: 10.1016/j.jmb.2022.167920. PMID:36528084 doi:https://dx.doi.org/10.1016/j.jmb.2022.167920

[1]

[2]

@@ Line 1: / Line 1: @@
 ==hnRNP A2/B1 RRMs in complex with single-stranded DNA==
-<StructureSection load='7wm3' size='340' side='right'caption='[[7wm3]]' scene=''>
+<StructureSection load='7wm3' size='340' side='right'caption='[[7wm3]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WM3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WM3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7wm3]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WM3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WM3 FirstGlance]. <br>
 </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=7wm3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wm3 OCA], [https://pdbe.org/7wm3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wm3 RCSB], [https://www.ebi.ac.uk/pdbsum/7wm3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wm3 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 ==
+Heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP A2/B1) has been identified as a nuclear DNA sensor. Upon viral infection, hnRNP A2/B1 recognizes pathogen-derived DNA as a homodimer, which is a prerequisite for its translocation to the cytoplasm to activate the interferon response. However, the DNA binding mechanism inducing hnRNP A2/B1 homodimerization is unknown. Here, we show the crystal structure of the RNA recognition motif (RRM) of hnRNP A2/B1 in complex with a U-shaped ssDNA, which mediates the formation of a newly observed protein dimer. Our biochemical assays and mutagenesis studies confirm that the hnRNP A2/B1 homodimer forms in solution by binding to pre-generated ssDNA or dsDNA with a U-shaped bulge. These results depict a potential functional state of hnRNP A2/B1 in antiviral immunity and other cellular processes.
+Structural Insight Into hnRNP A2/B1 Homodimerization and DNA Recognition.,Liu Y, Abula A, Xiao H, Guo H, Li T, Zheng L, Chen B, Nguyen HC, Ji X J Mol Biol. 2022 Dec 14;435(3):167920. doi: 10.1016/j.jmb.2022.167920. PMID:36528084<ref>PMID:36528084</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 7wm3" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Abula, A, Liu, Y, Guo, H, Li, T, Ji, X]]
+[[Category: Abula A]]
+[[Category: Guo H]]
+[[Category: Ji X]]
+[[Category: Li T]]
+[[Category: Liu Y]]

7wm3: Difference between revisions

Revision as of 07:48, 11 January 2023

hnRNP A2/B1 RRMs in complex with single-stranded DNA

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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