6FLK

Crystal structure of Cep120 C2C domain

6FLK の概要

• エントリーDOI: 10.2210/pdb6flk/pdb
• 分子名称: Cep120 (2 entities in total)
• 機能のキーワード: centriole, microtubule, cep120, c2 domain, structural protein
• 由来する生物種: homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 37074.65

構造登録者

Sharma, A.,Gerard, S.F.,Olieric, N.,Steinmetz, M.O. (登録日: 2018-01-26, 公開日: 2018-02-14, 最終更新日: 2024-05-08)

主引用文献

Sharma, A.,Gerard, S.F.,Olieric, N.,Steinmetz, M.O.
Cep120 promotes microtubule formation through a unique tubulin binding C2 domain.
J. Struct. Biol., 203:62-70, 2018

PubMed Abstract: Centrioles are microtubule-based structures that play essential roles in cell division and cilia biogenesis. Cep120 is an important protein for correct centriole formation and mutations in the Cep120 gene cause severe human diseases like Joubert syndrome and complex ciliopathies. Here, we show that Cep120 contains three consecutive C2 domains that are followed by a coiled-coil dimerization domain. Surprisingly, unlike the classical C2 domains, all three Cep120 C2 domains lack calcium- and phospholipid-binding activities. However, biophysical and biochemical assays revealed that the N-terminal Cep120 C2 domain (C2A) binds to both tubulin and microtubules, and promotes microtubule formation. Structural analyses coupled with mutagenesis identified a highly conserved, positively charged residue patch on the surface of Cep120 C2A, which mediates the interaction with tubulin and microtubules. Together, our results establish Cep120 C2A as a unique microtubule-binding domain. They further provide insights into the molecular mechanism of Cep120 during centriole biogenesis.

PubMed: 29398280
DOI: 10.1016/j.jsb.2018.01.009

実験手法

X-RAY DIFFRACTION (1.6 Å)