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| Hauptseite > Workflowsammlungen > Publikationsgebühren > Structural basis for the regulatory interactions of proapoptotic Par-4 > print |
| Hauptseite > Workflowsammlungen > Publikationsgebühren > Structural basis for the regulatory interactions of proapoptotic Par-4 > print |
| 001 | 834239 | ||
| 005 | 20220930130125.0 | ||
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| 100 | 1 | _ | |a Tiruttani Subhramanyam, Udaya Kumar |0 P:(DE-Juel1)131986 |b 0 |u fzj |
| 245 | _ | _ | |a Structural basis for the regulatory interactions of proapoptotic Par-4 |
| 260 | _ | _ | |a Houndmills, Basingstoke |c 2017 |b Nature Publishing Group |
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| 520 | _ | _ | |a 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. |
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| 700 | 1 | _ | |a Kubicek, Jan |0 P:(DE-HGF)0 |b 1 |
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| 773 | _ | _ | |a 10.1038/cdd.2017.76 |0 PERI:(DE-600)1496681-5 |p 1540–1547 |t Cell death and differentiation |v 24 |y 2017 |x 1350-9047 |
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