5ho4
From Proteopedia
(Difference between revisions)
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| - | ==Crystal structure of hnRNPA2B1 in | + | ==Crystal structure of hnRNPA2B1 in complex with 10-mer RNA== |
| - | <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. 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> | ||
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== 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. | [[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. | ||
| + | <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. | ||
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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®/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: Large Structures]] | ||
[[Category: Gan, J H]] | [[Category: Gan, J H]] | ||
[[Category: Ma, J B]] | [[Category: Ma, J B]] | ||
Revision as of 07:22, 23 May 2019
Crystal structure of hnRNPA2B1 in complex with 10-mer RNA
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