5LHW

Central Coiled-Coil Domain of Human STIL

Summary for 5LHW

• Entry DOI: 10.2210/pdb5lhw/pdb
• Descriptor: SCL-interrupting locus protein, HEXAETHYLENE GLYCOL (3 entities in total)
• Functional Keywords: centriole, structural protein
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm, cytosol : Q15468
• Total number of polymer chains: 1
• Total formula weight: 3481.99

Authors

Cottee, M.A.,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

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: 28202467
DOI: 10.1242/bio.024661

Experimental method

X-RAY DIFFRACTION (0.91 Å)