2mzt

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'''Unreleased structure'''
 
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The entry 2mzt is ON HOLD until Paper Publication
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==NMR structure of the RRM3 domain of Hrb1==
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<StructureSection load='2mzt' size='340' side='right'caption='[[2mzt]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2mzt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MZT FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2mzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mzt OCA], [https://pdbe.org/2mzt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mzt RCSB], [https://www.ebi.ac.uk/pdbsum/2mzt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mzt ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HRB1_YEAST HRB1_YEAST]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Metazoan SR and SR-like proteins are important regulatory factors in RNA splicing, export, translation and RNA decay. We determined the NMR structures and nucleic acid interaction modes of Gbp2 and Hrb1, two paralogous budding yeast proteins with similarities to mammalian SR proteins. Gbp2 RRM1 and RRM2 recognise preferentially RNAs containing the core motif GGUG. Sequence selectivity resides in a non-canonical interface in RRM2 that is highly related to the SRSF1 pseudoRRM. The atypical Gbp2/Hrb1 C-terminal RRM domains (RRM3) do not interact with RNA/DNA, likely because of their novel N-terminal extensions that block the canonical RNA binding interface. Instead, we discovered that RRM3 is crucial for interaction with the THO/TREX complex and identified key residues essential for this interaction. Moreover, Gbp2 interacts genetically with Tho2 as the double deletion shows a synthetic phenotype and preventing Gbp2 interaction with the THO/TREX complex partly supresses gene expression defect associated with inactivation of the latter complex. These findings provide structural and functional insights into the contribution of SR-like proteins in the post-transcriptional control of gene expression.
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Authors: Martinez-Lumbreras, S., Seraphin, B., Perez-Canadillas, J.
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Gbp2 interacts with THO/TREX through a novel type of RRM domain.,Martinez-Lumbreras S, Taverniti V, Zorrilla S, Seraphin B, Perez-Canadillas JM Nucleic Acids Res. 2015 Nov 23. pii: gkv1303. PMID:26602689<ref>PMID:26602689</ref>
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Description: NMR structure of the RRM3 domain of Hrb1
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Perez-Canadillas, J]]
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<div class="pdbe-citations 2mzt" style="background-color:#fffaf0;"></div>
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[[Category: Seraphin, B]]
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== References ==
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[[Category: Martinez-Lumbreras, S]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Martinez-Lumbreras S]]
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[[Category: Perez-Canadillas J]]
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[[Category: Seraphin B]]

Current revision

NMR structure of the RRM3 domain of Hrb1

PDB ID 2mzt

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