4xzr

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==Structure of yeast importin a bound to the membrane protein Nuclear Localization Signal sequence of INM protein Heh1==
==Structure of yeast importin a bound to the membrane protein Nuclear Localization Signal sequence of INM protein Heh1==
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<StructureSection load='4xzr' size='340' side='right' caption='[[4xzr]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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<StructureSection load='4xzr' size='340' side='right'caption='[[4xzr]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4xzr]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XZR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XZR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4xzr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XZR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XZR FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pvz|4pvz]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
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<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=4xzr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xzr OCA], [http://pdbe.org/4xzr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xzr RCSB], [http://www.ebi.ac.uk/pdbsum/4xzr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xzr ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4xzr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xzr OCA], [https://pdbe.org/4xzr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xzr RCSB], [https://www.ebi.ac.uk/pdbsum/4xzr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xzr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SRC1_YEAST SRC1_YEAST]] Plays a role in sister chromatid separation.<ref>PMID:11754482</ref> [[http://www.uniprot.org/uniprot/IMA1_YEAST IMA1_YEAST]] Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope. Seems to act as a cytosolic receptor for both simple and bipartite NLS motifs (By similarity).<ref>PMID:7565597</ref> <ref>PMID:10913188</ref> <ref>PMID:21075847</ref>
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[https://www.uniprot.org/uniprot/SRC1_YEAST SRC1_YEAST] Plays a role in sister chromatid separation.<ref>PMID:11754482</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Targeting of ER-synthesized membrane proteins to the inner nuclear membrane (INM) has long been explained by the diffusion-retention model. However, several INM proteins contain non-classical nuclear localization signal (NLS) sequences, which, in a few instances, have been shown to promote importin alpha/beta- and Ran-dependent translocation to the INM. Here, using structural and biochemical methods, we show that yeast INM proteins Heh2 and Src1/Heh1 contain bipartite import sequences that associate intimately with the minor NLS-binding pocket of yeast importin alpha and unlike classical NLSs efficiently displace the IBB domain in the absence of importin beta. In vivo, the intimate interactions at the minor NLS-binding pocket make the h2NLS highly efficient at recruiting importin alpha at the ER and drive INM localization of endogenous Heh2. Thus, h1/h2NLSs delineate a novel class of super-potent, IBB-like membrane protein NLSs, distinct from classical NLSs found in soluble cargos and of general interest in biology.
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Distinctive Properties of the Nuclear Localization Signals of Inner Nuclear Membrane Proteins Heh1 and Heh2.,Lokareddy RK, Hapsari RA, van Rheenen M, Pumroy RA, Bhardwaj A, Steen A, Veenhoff LM, Cingolani G Structure. 2015 May 19. pii: S0969-2126(15)00175-6. doi:, 10.1016/j.str.2015.04.017. PMID:26051712<ref>PMID:26051712</ref>
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==See Also==
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*[[Importin 3D structures|Importin 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4xzr" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cingolani, G]]
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[[Category: Large Structures]]
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[[Category: Lokareddy, R K]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Karyopherin]]
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[[Category: Cingolani G]]
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[[Category: Membrane protein]]
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[[Category: Lokareddy RK]]
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[[Category: Nl]]
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[[Category: Nuclear import]]
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Structure of yeast importin a bound to the membrane protein Nuclear Localization Signal sequence of INM protein Heh1

PDB ID 4xzr

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