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| | ==Gu_alpha_helicase== | | ==Gu_alpha_helicase== |
| - | <StructureSection load='3zin' size='340' side='right' caption='[[3zin]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='3zin' size='340' side='right'caption='[[3zin]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3zin]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZIN FirstGlance]. <br> | + | <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zio|3zio]], [[3zip|3zip]], [[3ziq|3ziq]], [[3zir|3zir]]</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]] 2Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA_helicase RNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.13 3.6.4.13] </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=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> |
| - | <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=3zin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zin OCA], [http://pdbe.org/3zin PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zin RCSB], [http://www.ebi.ac.uk/pdbsum/3zin PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zin ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/IMA2_MOUSE IMA2_MOUSE]] Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. [[http://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). | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Importin|Importin]] | + | *[[Importin 3D structures|Importin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: RNA helicase]] | + | [[Category: Mus musculus]] |
| - | [[Category: Chang, C W]] | + | [[Category: Chang C-W]] |
| - | [[Category: Counago, R M]] | + | [[Category: Counago RM]] |
| - | [[Category: Kobe, B]] | + | [[Category: Kobe B]] |
| - | [[Category: Williams, S J]] | + | [[Category: Williams SJ]] |
| - | [[Category: Transport protein-hydrolase complex]]
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| Structural highlights
Function
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).
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chang CW, Counago RM, Williams SJ, Boden M, Kobe B. Distinctive Conformation of Minor Site-Specific Nuclear Localization Signals Bound to Importin-alpha Traffic. 2013 Aug 2. doi: 10.1111/tra.12098. PMID:23910026 doi:10.1111/tra.12098
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