A bimodal distribution of two distinct categories of intrinsically disordered structures with separate functions in FG nucleoporins.

ABSTRACT: Nuclear pore complexes (NPCs) gate the only conduits for nucleocytoplasmic transport in eukaryotes. Their gate is formed by nucleoporins containing large intrinsically disordered domains with multiple phenylalanine-glycine repeats (FG domains). In combination, these are hypothesized to form a structurally and chemically homogeneous network of random coils at the NPC center, which sorts macromolecules by size and hydrophobicity. Instead, we found that FG domains are structurally and chemically heterogeneous. They adopt distinct categories of intrinsically disordered structures in non-random distributions. Some adopt globular, collapsed coil configurations and are characterized by a low charge content. Others are highly charged and adopt more dynamic, extended coil conformations. Interesting

SUBMITTER: Yamada J 

PROVIDER: S-EPMC2953916 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature