4xzr

</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=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>

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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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