4kf7

</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=4kf7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kf7 OCA], [https://pdbe.org/4kf7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kf7 RCSB], [https://www.ebi.ac.uk/pdbsum/4kf7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kf7 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Nucleocytoplasmic transport is mediated by nuclear pore complexes (NPCs) embedded in the nuclear envelope. About 30 different proteins (nucleoporins, nups) arrange around a central eightfold rotational axis to build the modular NPC. Nup188 and Nup192 are related and evolutionary conserved, large nucleoporins that are part of the NPC scaffold. Here we determine the structure of Nup188. The protein folds into an extended stack of helices where an N-terminal 130 kDa segment forms an intricate closed ring, while the C-terminal region is a more regular, superhelical structure. Overall, the structure has distant similarity with flexible S-shaped nuclear transport receptors (NTRs). Intriguingly, like NTRs, both Nup188 and Nup192 specifically bind FG-repeats and are able to translocate through NPCs by facilitated diffusion. This blurs the existing dogma of a clear distinction between stationary nups and soluble NTRs and suggests an evolutionary relationship between the NPC and the soluble nuclear transport machinery. DOI:http://dx.doi.org/10.7554/eLife.00745.001.

Scaffold nucleoporins Nup188 and Nup192 share structural and functional properties with nuclear transport receptors.,Andersen KR, Onischenko E, Tang JH, Kumar P, Chen JZ, Ulrich A, Liphardt JT, Weis K, Schwartz TU Elife. 2013 Jun 11;2:e00745. doi: 10.7554/eLife.00745. Print 2013. PMID:23795296<ref>PMID:23795296</ref>

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

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== References ==

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