Bending-Twisting Motions and Main Interactions in Nucleoplasmin Nuclear Import.

ABSTRACT: Alpha solenoid proteins play a key role in regulating the classical nuclear import pathway, recognizing a target protein and transporting it into the nucleus. Importin-α (Impα) is the solenoid responsible for cargo protein recognition, and it has been extensively studied by X-ray crystallography to understand the binding specificity. To comprehend the main motions of Impα and to extend the information about the critical interactions during carrier-cargo recognition, we surveyed different conformational states based on molecular dynamics (MD) and normal mode (NM) analyses. Our model of study was a crystallographic structure of Impα complexed with the classical nuclear localization sequence (cNLS) from nucleoplasmin (Npl), which was submitted to multiple 100 ns of MD simulations. Representat

SUBMITTER: Geraldo MT 

PROVIDER: S-EPMC4892583 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature