1di2: Difference between revisions

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 <StructureSection load='1di2' size='340' side='right'caption='[[1di2]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1di2]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/African_clawed_frog African clawed frog]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DI2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1di2]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DI2 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=1di2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1di2 OCA], [https://pdbe.org/1di2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1di2 RCSB], [https://www.ebi.ac.uk/pdbsum/1di2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1di2 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</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=1di2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1di2 OCA], [https://pdbe.org/1di2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1di2 RCSB], [https://www.ebi.ac.uk/pdbsum/1di2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1di2 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/PRKAB_XENLA PRKAB_XENLA]] Activates eif2ak2/pkr in the absence of double-stranded RNA (dsRNA), leading to phosphorylation of eif2s1/efi2-alpha and inhibition of translation and induction of apoptosis. Required for siRNA production by dicer1 and for subsequent siRNA-mediated post-transcriptional gene silencing. Does not seem to be required for processing of pre-miRNA to miRNA by dicer1 (By similarity).
+[https://www.uniprot.org/uniprot/PRKAB_XENLA PRKAB_XENLA] Activates eif2ak2/pkr in the absence of double-stranded RNA (dsRNA), leading to phosphorylation of eif2s1/efi2-alpha and inhibition of translation and induction of apoptosis. Required for siRNA production by dicer1 and for subsequent siRNA-mediated post-transcriptional gene silencing. Does not seem to be required for processing of pre-miRNA to miRNA by dicer1 (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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=1di2 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Protein interactions with double-stranded RNA (dsRNA) are critical for many cell processes; however, in contrast to protein-dsDNA interactions, surprisingly little is known about the molecular basis of protein-dsRNA interactions. A large and diverse class of proteins that bind dsRNA do so by utilizing an approximately 70 amino acid motif referred to as the dsRNA-binding domain (dsRBD). We have determined a 1.9 A resolution crystal structure of the second dsRBD of Xenopus laevis RNA-binding protein A complexed with dsRNA. The structure shows that the protein spans 16 bp of dsRNA, interacting with two successive minor grooves and across the intervening major groove on one face of a primarily A-form RNA helix. The nature of these interactions explains dsRBD specificity for dsRNA (over ssRNA or dsDNA) and the apparent lack of sequence specificity. Interestingly, the dsRBD fold resembles a portion of the conserved core structure of a family of polynucleotidyl transferases that includes RuvC, MuA transposase, retroviral integrase and RNase H. Structural comparisons of the dsRBD-dsRNA complex and models proposed for polynucleotidyl transferase-nucleic acid complexes suggest that similarities in nucleic acid binding also exist between these families of proteins.
-Molecular basis of double-stranded RNA-protein interactions: structure of a dsRNA-binding domain complexed with dsRNA.,Ryter JM, Schultz SC EMBO J. 1998 Dec 15;17(24):7505-13. PMID:9857205<ref>PMID:9857205</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1di2" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[P19|P19]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: African clawed frog]]
 [[Category: Large Structures]]
-[[Category: Ryter, J M]]
+[[Category: Xenopus laevis]]
-[[Category: Schultz, S C]]
+[[Category: Ryter JM]]
-[[Category: Double stranded rna]]
+[[Category: Schultz SC]]
-[[Category: Protein-rna complex]]
-[[Category: Protein-rna interaction]]
-[[Category: Rna binding protein-rna complex]]
-[[Category: Rna-bining protein]]