4dkk

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4dkk]] is a 1 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=4DKK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DKK FirstGlance]. <br>
<table><tr><td colspan='2'>[[4dkk]] is a 1 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=4DKK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DKK FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></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]] 1.701&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></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=4dkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dkk OCA], [https://pdbe.org/4dkk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dkk RCSB], [https://www.ebi.ac.uk/pdbsum/4dkk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dkk ProSAT]</span></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=4dkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dkk OCA], [https://pdbe.org/4dkk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dkk RCSB], [https://www.ebi.ac.uk/pdbsum/4dkk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dkk ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/STAU1_HUMAN STAU1_HUMAN]] Binds double-stranded RNA (regardless of the sequence) and tubulin. May play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site.
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[https://www.uniprot.org/uniprot/STAU1_HUMAN STAU1_HUMAN] Binds double-stranded RNA (regardless of the sequence) and tubulin. May play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Staufen1 (STAU1)-mediated mRNA decay (SMD) degrades mammalian-cell mRNAs that bind the double-stranded RNA (dsRNA)-binding protein STAU1 in their 3' untranslated region. We report a new motif, which typifies STAU homologs from all vertebrate classes, that is responsible for human STAU1 (hSTAU1) homodimerization. Our crystal structure and mutagenesis analyses reveal that this motif, which we named the Staufen-swapping motif (SSM), and the dsRNA-binding domain 5 ('RBD'5) mediate protein dimerization: the two SSM alpha-helices of one molecule interact primarily through a hydrophobic patch with the two 'RBD'5 alpha-helices of a second molecule. 'RBD'5 adopts the canonical alpha-beta-beta-beta-alpha fold of a functional RBD, but it lacks residues and features required to bind duplex RNA. In cells, SSM-mediated hSTAU1 dimerization increases the efficiency of SMD by augmenting hSTAU1 binding to the ATP-dependent RNA helicase hUPF1. Dimerization regulates keratinocyte-mediated wound healing and many other cellular processes.
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Staufen1 dimerizes through a conserved motif and a degenerate dsRNA-binding domain to promote mRNA decay.,Gleghorn ML, Gong C, Kielkopf CL, Maquat LE Nat Struct Mol Biol. 2013 Apr;20(4):515-24. doi: 10.1038/nsmb.2528. Epub 2013 Mar, 24. PMID:23524536<ref>PMID:23524536</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 4dkk" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

The X-ray Crystal Structure of the Human STAU1 SSM-'RBD'5 Domain-Swapped Dimer

PDB ID 4dkk

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