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@ARTICLE{TiruttaniSubhramanyam:834239,
author = {Tiruttani Subhramanyam, Udaya Kumar and Kubicek, Jan and
Eidhoff, Ulf Benno and Labahn, Jörg},
title = {{S}tructural basis for the regulatory interactions of
proapoptotic {P}ar-4},
journal = {Cell death and differentiation},
volume = {24},
issn = {1350-9047},
address = {Houndmills, Basingstoke},
publisher = {Nature Publishing Group},
reportid = {FZJ-2017-04221},
pages = {1540–1547},
year = {2017},
abstract = {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.},
cin = {ICS-6},
ddc = {570},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {551 - Functional Macromolecules and Complexes (POF3-551)},
pid = {G:(DE-HGF)POF3-551},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000407506500009},
pubmed = {pmid:28622290},
doi = {10.1038/cdd.2017.76},
url = {https://juser.fz-juelich.de/record/834239},
}