5FIY

crystal structure of coiled coil domain of PAWR

Summary for 5FIY

• Entry DOI: 10.2210/pdb5fiy/pdb
• Descriptor: PRKC APOPTOSIS WT1 REGULATOR PROTEIN, POTASSIUM ION (3 entities in total)
• Functional Keywords: apoptosis
• Biological source: RATTUS NORVEGICUS (NORWAY RAT)
• Cellular location: Cytoplasm : Q62627
• Total number of polymer chains: 7
• Total formula weight: 87513.45

Authors

Tiruttani Subhramanyam, U.K.,Kubicek, J.,Eidhoff, U.B.,Labahn, J. (deposition date: 2015-10-03, release date: 2016-11-16, Last modification date: 2024-05-01)

Primary citation

Tiruttani Subhramanyam, U.K.,Kubicek, J.,Eidhoff, U.B.,Labahn, J.
Structural basis for the regulatory interactions of proapoptotic Par-4.
Cell Death Differ., 24:1540-1547, 2017

PubMed 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-4), 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-4 contains the homodimerization subdomain. This structure includes a nuclear export signal (Par-4) 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-4). These heteromer models also displayed NES masking capacity and therefore the ability to influence intracellular localization.

PubMed: 28622290
DOI: 10.1038/cdd.2017.76

Experimental method

X-RAY DIFFRACTION (3 Å)