4xzr
From Proteopedia
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| - | ''' | + | ==Structure of yeast importin a bound to the membrane protein Nuclear Localization Signal sequence of INM protein Heh1== |
| + | <StructureSection load='4xzr' size='340' side='right' caption='[[4xzr]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pvz|4pvz]]</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=4xzr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xzr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xzr RCSB], [http://www.ebi.ac.uk/pdbsum/4xzr PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Cingolani, G]] | [[Category: Cingolani, G]] | ||
| + | [[Category: Lokareddy, R K]] | ||
| + | [[Category: Karyopherin]] | ||
| + | [[Category: Membrane protein]] | ||
| + | [[Category: Nl]] | ||
| + | [[Category: Nuclear import]] | ||
Revision as of 15:00, 17 June 2015
Structure of yeast importin a bound to the membrane protein Nuclear Localization Signal sequence of INM protein Heh1
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