5x8n

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'''Unreleased structure'''
 
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The entry 5x8n is ON HOLD until Paper Publication
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==Crystal structure of mouse importin-alpha1 bound to the nuclear localization signal of Epstein-Barr virus EBNA-LP protein==
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<StructureSection load='5x8n' size='340' side='right' caption='[[5x8n]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5x8n]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X8N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X8N FirstGlance]. <br>
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</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=5x8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x8n OCA], [http://pdbe.org/5x8n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x8n RCSB], [http://www.ebi.ac.uk/pdbsum/5x8n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x8n ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/IMA1_MOUSE IMA1_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/EBNA5_EBVB9 EBNA5_EBVB9]] Plays an important role in the establishment of B-cell immortalization by acting as an EBNA2 coactivator. This transcriptional activation preferentially enhances the expression of the major viral protein LMP1. The interaction between EBNA-LP and host SP100 correlates with coactivation of EBNA2 and the relocalization of SP100 from PML nuclear bodies into nucleoplasm.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Epstein-Barr virus EBNA-LP protein is a transcriptional coactivator of EBNA2. Efficient nuclear localization of EBNA-LP is essential for cooperation with EBNA2. Here, we report the crystal structure of the nuclear import adaptor importin-alpha1 bound to the nuclear localization signal (NLS) of EBNA-LP that shows EBNA-LP residues 44-RRVRRR-49 binding to the major NLS-binding site at the P0-P5 positions. In contrast to previously characterized classical NLSs that invariably have a basic residue [either lysine (in the vast majority of cases) or arginine] at the P2 position, the EBNA-LP NLS is unique in that it has valine at the P2 position. The loss of the critical P2 lysine (or arginine) is compensated by arginine at the P0 position in the EBNA-LP NLS.
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Authors:
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Crystal structure of importin-alpha bound to the nuclear localization signal of Epstein-Barr virus EBNA-LP protein.,Nakada R, Matsuura Y Protein Sci. 2017 Apr 6. doi: 10.1002/pro.3173. PMID:28383161<ref>PMID:28383161</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5x8n" 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>
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[[Category: Matsuura, Y]]
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[[Category: Nakada, R]]
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[[Category: Ebna-lp]]
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[[Category: Epstein-barr virus]]
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[[Category: Importin]]
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[[Category: Nl]]
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[[Category: Protein transport-transcription complex]]

Revision as of 13:06, 19 April 2017

Crystal structure of mouse importin-alpha1 bound to the nuclear localization signal of Epstein-Barr virus EBNA-LP protein

5x8n, resolution 2.15Å

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