Nuclear pore complex protein sequences determine overall copolymer brush structure and function.

ABSTRACT: The transport of cargo across the nuclear membrane is highly selective and accomplished by a poorly understood mechanism involving hundreds of nucleoporins lining the inside of the nuclear pore complex (NPC). Currently, there is no clear picture of the overall structure formed by this collection of proteins within the pore, primarily due to their disordered nature. We perform coarse-grained simulations of both individual nucleoporins and grafted rings of nups mimicking the in vivo geometry of the NPC and supplement this with polymer brush modeling. Our results indicate that different regions or blocks of an individual NPC protein can have distinctly different forms of disorder and that this property appears to be a conserved functional feature. Furthermore, this block structure at the indi

SUBMITTER: Ando D 

PROVIDER: S-EPMC4017316 | biostudies-literature | 2014 May

REPOSITORIES: biostudies-literature