View source for 3zin


==Gu_alpha_helicase==
<StructureSection load='3zin' size='340' side='right'caption='[[3zin]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zin]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZIN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#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=3zin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zin OCA], [https://pdbe.org/3zin PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zin RCSB], [https://www.ebi.ac.uk/pdbsum/3zin PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zin ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DDX21_MOUSE DDX21_MOUSE] Can unwind double-stranded RNA (helicase) and can fold or introduce a secondary structure to a single-stranded RNA (foldase). Functions as cofactor for JUN-activated transcription (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nuclear localization signals (NLSs) contain one or two clusters of basic residues and are recognized by the import receptor importin-alpha. There are two NLS-binding sites (major and minor) on importin-alpha and the major NLS-binding site is considered to be the primary binding site. Here, we used crystallographic and biochemical methods to investigate the binding between importin-alpha and predicted "minor site-specific" NLSs: four peptide library-derived peptides, and the NLS from mouse RNA helicase II/Gualpha. The crystal structures reveal that these atypical NLSs indeed preferentially bind to the minor NLS-binding site. Unlike previously characterized NLSs, the C-terminal residues of these NLSs form an alpha-helical turn, stabilized by internal H-bond and cation-pi interactions between the aromatic residues from the NLSs and the positively-charged residues from importin-alpha. This helical turn sterically hinders binding at the major NLS-binding site, explaining the minor-site preference. Our data suggest the sequence RXXKR[K/X][F/Y/W]XXAF as the optimal minor NLS-binding site-specific motif, which may help identify novel proteins with atypical NLSs.

Distinctive Conformation of Minor Site-Specific Nuclear Localization Signals Bound to Importin-alpha,Chang CW, Counago RM, Williams SJ, Boden M, Kobe B Traffic. 2013 Aug 2. doi: 10.1111/tra.12098. PMID:23910026<ref>PMID:23910026</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zin" style="background-color:#fffaf0;"></div>

==See Also==
*[[Importin 3D structures|Importin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Chang C-W]]
[[Category: Counago RM]]
[[Category: Kobe B]]
[[Category: Williams SJ]]