4jq5

</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=4jq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jq5 OCA], [https://pdbe.org/4jq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jq5 RCSB], [https://www.ebi.ac.uk/pdbsum/4jq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jq5 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The nuclear pore complex (NPC) constitutes the sole gateway for bidirectional nucleocytoplasmic transport. We present the reconstitution and interdisciplinary analyses of the ~425-kDa inner ring complex (IRC), which forms the central transport channel and diffusion barrier of the NPC, revealing its interaction network and equimolar stoichiometry. The Nsp1*Nup49*Nup57 channel nucleoporin hetero-trimer (CNT) attaches to the IRC solely through the adaptor nucleoporin Nic96. The CNT*Nic96 structure reveals that Nic96 functions as an assembly sensor that recognizes the three dimensional architecture of the CNT, thereby mediating the incorporation of a defined CNT state into the NPC. We propose that the IRC adopts a relatively rigid scaffold that recruits the CNT to primarily form the diffusion barrier of the NPC, rather than enabling channel dilation.

Architecture of the fungal nuclear pore inner ring complex.,Stuwe T, Bley CJ, Thierbach K, Petrovic S, Schilbach S, Mayo DJ, Perriches T, Rundlet EJ, Jeon YE, Collins LN, Huber FM, Lin DH, Paduch M, Koide A, Lu V, Fischer J, Hurt E, Koide S, Kossiakoff AA, Hoelz A Science. 2015 Aug 27. pii: aac9176. PMID:26316600<ref>PMID:26316600</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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