4MJS
crystal structure of a PB1 complex
Summary for 4MJS
| Entry DOI | 10.2210/pdb4mjs/pdb |
| Descriptor | Protein kinase C zeta type, Sequestosome-1, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | pb1 domain, pb1 heterodimer and protein interaction, transferase-protein binding complex, transferase/protein binding |
| Biological source | Rattus norvegicus (brown rat,rat,rats) More |
| Cellular location | Cytoplasm : P09217 Q13501 |
| Total number of polymer chains | 24 |
| Total formula weight | 262206.60 |
| Authors | Ren, J.,Wang, Z.X.,Wu, J.W. (deposition date: 2013-09-04, release date: 2014-08-27, Last modification date: 2023-11-08) |
| Primary citation | Ren, J.,Wang, J.,Wang, Z.X.,Wu, J.W. Structural and biochemical insights into the homotypic PB1-PB1 complex between PKC zeta and p62 Sci China Life Sci, 57:69-80, 2014 Cited by PubMed Abstract: The atypical PKC isoforms (ζ and ı) play essential roles in regulating various cellular processes. Both the hetero-interaction between PKCζ and p62 through their N-terminal PB1 domains and the homo-oligomerization of p62 via its PB1 domain are critical for the activation of NF-κB signaling; however, the molecular mechanisms concerning the formation and regulation of these homotypic complexes remain unclear. Here we determined the crystal structure of PKCζ-PB1 in complex with a monomeric p62-PB1 mutant, where the massive electrostatic interactions between the acidic OPCA motif of PKCζ-PB1 and the basic surface of p62-PB1, as well as additional hydrogen bonds, ensure the formation of a stable and specific complex. The PKCζ-p62 interaction is interfered with the modification of a specific Cys of PKCζ by the antiarthritis drug aurothiomalate, though all four cysteine residues in the PKCζ-PB1 domain can be modified in in vitro assay. In addition, detailed structural and biochemical analyses demonstrate that the PB1 domains of aPKCs belong to the type I group, which can depolymerize the high-molecular-weight p62 aggregates into homo-oligomers of lower order. These data together unravel the molecular mechanisms of the homo-or hetero-interactions between p62 and PKCζ and provide the basis for designing inhibitors of NF-κB signaling. PubMed: 24369353DOI: 10.1007/s11427-013-4592-z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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