%0 Journal Article
%A Tiruttani Subhramanyam, Udaya Kumar
%A Kubicek, Jan
%A Eidhoff, Ulf Benno
%A Labahn, Jörg
%T Structural basis for the regulatory interactions of proapoptotic Par-4
%J Cell death and differentiation
%V 24
%@ 1350-9047
%C Houndmills, Basingstoke
%I Nature Publishing Group
%M FZJ-2017-04221
%P 1540–1547
%D 2017
%X Par-4 is a unique proapoptotic protein with the ability to induce apoptosis selectively in cancer cells. The X-ray crystal structure of the C-terminal domain of Par-4 (Par-4CC), which regulates its apoptotic function, was obtained by MAD phasing. Par-4 homodimerizes by forming a parallel coiled-coil structure. The N-terminal half of Par-4CC contains the homodimerization subdomain. This structure includes a nuclear export signal (Par-4NES) sequence, which is masked upon dimerization indicating a potential mechanism for nuclear localization. The heteromeric-interaction models specifically showed that charge interaction is an important factor in the stability of heteromers of the C-terminal leucine zipper subdomain of Par-4 (Par-4LZ). These heteromer models also displayed NES masking capacity and therefore the ability to influence intracellular localization.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000407506500009
%$ pmid:28622290
%R 10.1038/cdd.2017.76
%U https://juser.fz-juelich.de/record/834239