1stu

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[[Image:1stu.gif|left|200px]]
 
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==DOUBLE STRANDED RNA BINDING DOMAIN==
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The line below this paragraph, containing "STRUCTURE_1stu", creates the "Structure Box" on the page.
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<StructureSection load='1stu' size='340' side='right'caption='[[1stu]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1stu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1STU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1STU FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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=1stu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1stu OCA], [https://pdbe.org/1stu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1stu RCSB], [https://www.ebi.ac.uk/pdbsum/1stu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1stu ProSAT]</span></td></tr>
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{{STRUCTURE_1stu| PDB=1stu | SCENE= }}
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</table>
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== Function ==
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'''DOUBLE STRANDED RNA BINDING DOMAIN'''
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[https://www.uniprot.org/uniprot/STAU_DROME STAU_DROME] Required both for the localization of maternal determinants to the posterior pole of the egg, oskar (osk) RNA, and for correct localization to the anterior pole, anchoring bicoid (bcd) RNA. Osk protein is required to keep osk RNA and stau protein at the posterior pole. Stau-bcd complexes form particles that show a microtubule-dependent localization.<ref>PMID:1712672</ref> <ref>PMID:8001156</ref> <ref>PMID:10698941</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/st/1stu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1stu ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
The double-stranded RNA binding domain (dsRBD) is an approximately 65 amino acid motif that is found in a variety of proteins that interact with double-stranded (ds) RNA, such as Escherichia coli RNase III and the dsRNA-dependent kinase, PKR. Drosophila staufen protein contains five copies of this motif, and the third of these binds dsRNA in vitro. Using multinuclear/multidimensional NMR methods, we have determined that staufen dsRBD3 forms a compact protein domain with an alpha-beta-beta-beta-alpha structure in which the two alpha-helices lie on one face of a three-stranded anti-parallel beta-sheet. This structure is very similar to that of the N-terminal domain of a prokaryotic ribosomal protein S5. Furthermore, the consensus derived from all known S5p family sequences shares several conserved residues with the dsRBD consensus sequence, indicating that the two domains share a common evolutionary origin. Using in vitro mutagenesis, we have identified several surface residues which are important for the RNA binding of the dsRBD, and these all lie on the same side of the domain. Two residues that are essential for RNA binding, F32 and K50, are also conserved in the S5 protein family, suggesting that the two domains interact with RNA in a similar way.
The double-stranded RNA binding domain (dsRBD) is an approximately 65 amino acid motif that is found in a variety of proteins that interact with double-stranded (ds) RNA, such as Escherichia coli RNase III and the dsRNA-dependent kinase, PKR. Drosophila staufen protein contains five copies of this motif, and the third of these binds dsRNA in vitro. Using multinuclear/multidimensional NMR methods, we have determined that staufen dsRBD3 forms a compact protein domain with an alpha-beta-beta-beta-alpha structure in which the two alpha-helices lie on one face of a three-stranded anti-parallel beta-sheet. This structure is very similar to that of the N-terminal domain of a prokaryotic ribosomal protein S5. Furthermore, the consensus derived from all known S5p family sequences shares several conserved residues with the dsRBD consensus sequence, indicating that the two domains share a common evolutionary origin. Using in vitro mutagenesis, we have identified several surface residues which are important for the RNA binding of the dsRBD, and these all lie on the same side of the domain. Two residues that are essential for RNA binding, F32 and K50, are also conserved in the S5 protein family, suggesting that the two domains interact with RNA in a similar way.
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==About this Structure==
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NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5.,Bycroft M, Grunert S, Murzin AG, Proctor M, St Johnston D EMBO J. 1995 Jul 17;14(14):3563-71. PMID:7628456<ref>PMID:7628456</ref>
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1STU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1STU OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5., Bycroft M, Grunert S, Murzin AG, Proctor M, St Johnston D, EMBO J. 1995 Jul 17;14(14):3563-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7628456 7628456]
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</div>
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<div class="pdbe-citations 1stu" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bycroft, M.]]
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[[Category: Bycroft M]]
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[[Category: Staufen]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:07:38 2008''
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Current revision

DOUBLE STRANDED RNA BINDING DOMAIN

PDB ID 1stu

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