5c3l

Publication Abstract from PubMed

Nuclear pore complexes (NPCs) conduct nucleocytoplasmic transport and gain transport selectivity through nucleoporin FG domains. Here, we report a structural analysis of the FG Nup62*58*54 complex, which is a crucial component of the transport system. It comprises a approximately 13 nm long trimerization interface with an unusual 2W3F coil, a canonical heterotrimeric coiled coil, and a kink that enforces a compact six-helix bundle. Nup54 also contains a ferredoxin-like domain. We further identified a heterotrimeric Nup93-binding module for NPC anchorage. The quaternary structure alternations in the Nup62 complex, which were previously proposed to trigger a general NPC-gating, are incompatible with the trimer structure. We suggest that the highly elongated Nup62 complex projects barrier-forming FG-repeats far into the central NPC channel, supporting a barrier that guards the entire cross-section.

Crystal structure of the metazoan Nup62*Nup58*Nup54 nucleoporin complex.,Chug H, Trakhanov S, Hulsmann BB, Pleiner T, Gorlich D Science. 2015 Aug 20. pii: aac7420. PMID:26292704^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.