TY  - JOUR
AU  - Tiruttani Subhramanyam, Udaya Kumar
AU  - Kubicek, Jan
AU  - Eidhoff, Ulf Benno
AU  - Labahn, Jörg
TI  - Structural basis for the regulatory interactions of proapoptotic Par-4
JO  - Cell death and differentiation
VL  - 24
SN  - 1350-9047
CY  - Houndmills, Basingstoke
PB  - Nature Publishing Group
M1  - FZJ-2017-04221
SP  - 1540–1547
PY  - 2017
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000407506500009
C6  - pmid:28622290
DO  - DOI:10.1038/cdd.2017.76
UR  - https://juser.fz-juelich.de/record/834239
ER  -