Structural highlights
Publication Abstract from PubMed
The nuclear pore complex encloses a central channel for nucleocytoplasmic transport, which is thought to consist of three nucleoporins, Nup54, Nup58, and Nup62. However, the structure and composition of the channel are elusive. We determined the crystal structures of the interacting domains between these nucleoporins and pieced together the molecular architecture of the mammalian transport channel. Located in the channel midplane is a flexible Nup54Nup58 ring that can undergo large rearrangements yielding diameter changes from approximately 20 to approximately 40 nm. Nup62Nup54 triple helices project alternately up and down from either side of the midplane ring and form nucleoplasmic and cytoplasmic entries. The channel consists of as many as 224 copies of the three nucleoporins, amounting to a molar mass of 12.3 MDa and contributing 256 phenylalanine-glycine repeat regions. We propose that the occupancy of these repeat regions with transport receptors modulates ring diameter and transport activity.
Molecular architecture of the transport channel of the nuclear pore complex.,Solmaz SR, Chauhan R, Blobel G, Melcak I Cell. 2011 Oct 28;147(3):590-602. PMID:22036567[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Solmaz SR, Chauhan R, Blobel G, Melcak I. Molecular architecture of the transport channel of the nuclear pore complex. Cell. 2011 Oct 28;147(3):590-602. PMID:22036567 doi:10.1016/j.cell.2011.09.034
