Nuclear import factors importin alpha and importin beta undergo mutually induced conformational changes upon association. Academic Article uri icon

Overview

abstract

  • A heterodimer of importin alpha and importin beta accomplishes the nuclear import of proteins carrying classical nuclear localization signals (NLS). The interaction between the two import factors is mediated by the IBB domain of importin alpha and involves an extended recognition surface as shown by X-ray crystallography. Using a combination of biochemical and biophysical techniques we have investigated the formation of the importin beta:IBB domain complex in solution. Our data suggest that upon binding to the IBB domain, importin beta adopts a compact, proteolytically resistant conformation, while simultaneously the IBB domain folds into an alpha helix. We suggest a model to describe how these dual mutually induced conformational changes may orchestrate the nuclear import of NLS cargo in vivo.

publication date

  • November 10, 2000

Research

keywords

  • Nuclear Proteins

Identity

Scopus Document Identifier

  • 0034634450

Digital Object Identifier (DOI)

  • 10.1016/s0014-5793(00)02154-2

PubMed ID

  • 11078895

Additional Document Info

volume

  • 484

issue

  • 3