title: Transport-related structures and processes of the nuclear pore complex studied through molecular dynamics.
abstract: Nuclear pore complexes (NPCs) are selectively gated pathways between nucleoplasm and cytoplasm. Whereas small molecules can diffuse freely through NPCs, large molecules (>40 kD) can pass only when bound to transport receptors. The NPC central channel is filled with disordered proteins, rich in phenylalanine-glycine (FG) repeats, referred to as FG-nups. Our simulations, carried out at coarse-grained and all-atom levels, show that arrays of FG-nups tethered to a planar surface, at an FG-repeat density found in the NPC, form dynamic brush-like structures of multiprotein bundles, whereas individual FG-nups form dynamic globular structures. More than half of the FG-repeats are found on the surface of the bundles, offering a favorable environment for transport receptors. Binding to FG-repeats and a sliding motion of NTF2 induced by binding and unbinding to phenylalanines were observed when adding this transport receptor into one of the brush-like structures.
authors.affiliation: Beckman Institute for Advanced Science and Technology and Department of Physics, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
authors.forename: Lingling
authors.initials: L
authors.lastname: Miao
authors.forename: Klaus
authors.initials: K
authors.lastname: Schulten
mesh_terms: D002467:Cell Nucleus / Q000378:metabolism; D003198:Computer Simulation; D003593:Cytoplasm / Q000378:metabolism; D008958:Models, Molecular; D022022:Nuclear Pore / Q000737:chemistry* / Q000378:metabolism; D029543:Nucleocytoplasmic Transport Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: D029543:Nucleocytoplasmic Transport Proteins