5LHY

PB3 Domain of Human PLK4 (apo)

5LHY の概要

• エントリーDOI: 10.2210/pdb5lhy/pdb
• 分子名称: Serine/threonine-protein kinase PLK4 (1 entity in total)
• 機能のキーワード: polo box domain, centriole, transferase, structural protein
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole : O00444
• タンパク質・核酸の鎖数: 60
• 化学式量合計: 594911.46

構造登録者

Cottee, M.A.,Johnson, S.,Lea, S.M. (登録日: 2016-07-13, 公開日: 2017-03-01, 最終更新日: 2024-01-10)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.31 Å)