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000834239 1001_ $$0P:(DE-Juel1)131986$$aTiruttani Subhramanyam, Udaya Kumar$$b0$$ufzj
000834239 245__ $$aStructural basis for the regulatory interactions of proapoptotic Par-4
000834239 260__ $$aHoundmills, Basingstoke$$bNature Publishing Group$$c2017
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000834239 520__ $$aPar-4 is a unique proapoptotic protein with the ability to induce apoptosis selectively in cancer cells. The X-ray crystal structure of the C-terminal domain of Par-4 (Par-4CC), which regulates its apoptotic function, was obtained by MAD phasing. Par-4 homodimerizes by forming a parallel coiled-coil structure. The N-terminal half of Par-4CC contains the homodimerization subdomain. This structure includes a nuclear export signal (Par-4NES) sequence, which is masked upon dimerization indicating a potential mechanism for nuclear localization. The heteromeric-interaction models specifically showed that charge interaction is an important factor in the stability of heteromers of the C-terminal leucine zipper subdomain of Par-4 (Par-4LZ). These heteromer models also displayed NES masking capacity and therefore the ability to influence intracellular localization.
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000834239 7001_ $$0P:(DE-HGF)0$$aKubicek, Jan$$b1
000834239 7001_ $$0P:(DE-HGF)0$$aEidhoff, Ulf Benno$$b2
000834239 7001_ $$0P:(DE-Juel1)131973$$aLabahn, Jörg$$b3$$eCorresponding author$$ufzj
000834239 773__ $$0PERI:(DE-600)1496681-5$$a10.1038/cdd.2017.76$$p1540–1547$$tCell death and differentiation$$v24$$x1350-9047$$y2017
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