1di2

<StructureSection load='1di2' size='340' side='right' caption='[[1di2]], [[Resolution|resolution]] 1.90&Aring;' scene=''>

<table><tr><td colspan='2'>[[1di2]] is a 6 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1di2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1di2 OCA], [http://pdbe.org/1di2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1di2 RCSB], [http://www.ebi.ac.uk/pdbsum/1di2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1di2 ProSAT]</span></td></tr>

[[http://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).

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== 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>

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<div class="pdbe-citations 1di2" style="background-color:#fffaf0;"></div>

*[[User:Wayne Decatur/Plant Viral Protein p19 Suppression of RNA Silencing|User:Wayne Decatur/Plant Viral Protein p19 Suppression of RNA Silencing]]

[[Category: African clawed frog]]

[[Category: Ryter, J M]]

[[Category: Schultz, S C]]

[[Category: Double stranded rna]]

[[Category: Rna-bining protein]]