5LHY
PB3 Domain of Human PLK4 (apo)
Summary for 5LHY
| Entry DOI | 10.2210/pdb5lhy/pdb |
| Descriptor | Serine/threonine-protein kinase PLK4 (1 entity in total) |
| Functional Keywords | polo box domain, centriole, transferase, structural protein |
| Biological source | Homo sapiens (Human) |
| Cellular location | Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole : O00444 |
| Total number of polymer chains | 60 |
| Total formula weight | 594911.46 |
| Authors | Cottee, M.A.,Johnson, S.,Lea, S.M. (deposition date: 2016-07-13, release date: 2017-03-01, Last modification date: 2024-01-10) |
| Primary citation | Cottee, M.A.,Johnson, S.,Raff, J.W.,Lea, S.M. A key centriole assembly interaction interface between human PLK4 and STIL appears to not be conserved in flies. Biol Open, 6:381-389, 2017 Cited by PubMed Abstract: A small number of proteins form a conserved pathway of centriole duplication. In humans and flies, the binding of PLK4/Sak to STIL/Ana2 initiates daughter centriole assembly. In humans, this interaction is mediated by an interaction between the Polo-Box-3 (PB3) domain of PLK4 and the coiled-coil domain of STIL (HsCCD). We showed previously that the Ana2 coiled-coil domain (DmCCD) is essential for centriole assembly, but it forms a tight parallel tetramer that likely precludes an interaction with PB3. Here, we show that the isolated HsCCD and HsPB3 domains form a mixture of homo-multimers , but these readily dissociate when mixed to form the previously described 1:1 HsCCD:HsPB3 complex. In contrast, although PB3 (DmPB3) adopts a canonical polo-box fold, it does not detectably interact with DmCCD Thus, surprisingly, a key centriole assembly interaction interface appears to differ between humans and flies. PubMed: 28202467DOI: 10.1242/bio.024661 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.31 Å) |
Structure validation
Download full validation report
