6HXT

Crystal structure of the head domain of human CCDC61

6HXT の概要

• エントリーDOI: 10.2210/pdb6hxt/pdb
• 分子名称: Coiled-coil domain-containing protein 61 (2 entities in total)
• 機能のキーワード: centrosome, cilia, scaffold protein, protfilament, structural protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 50211.49

構造登録者

Ochi, T.,Blundell, T.L.,van Breugel, M. (登録日: 2018-10-18, 公開日: 2020-04-29, 最終更新日: 2024-10-23)

主引用文献

Ochi, T.,Quarantotti, V.,Lin, H.,Jullien, J.,Rosa E Silva, I.,Boselli, F.,Barnabas, D.D.,Johnson, C.M.,McLaughlin, S.H.,Freund, S.M.V.,Blackford, A.N.,Kimata, Y.,Goldstein, R.E.,Jackson, S.P.,Blundell, T.L.,Dutcher, S.K.,Gergely, F.,van Breugel, M.
CCDC61/VFL3 Is a Paralog of SAS6 and Promotes Ciliary Functions.
Structure, 28:674-, 2020

PubMed Abstract: Centrioles are cylindrical assemblies whose peripheral microtubule array displays a 9-fold rotational symmetry that is established by the scaffolding protein SAS6. Centriole symmetry can be broken by centriole-associated structures, such as the striated fibers in Chlamydomonas that are important for ciliary function. The conserved protein CCDC61/VFL3 is involved in this process, but its exact role is unclear. Here, we show that CCDC61 is a paralog of SAS6. Crystal structures of CCDC61 demonstrate that it contains two homodimerization interfaces that are similar to those found in SAS6, but result in the formation of linear filaments rather than rings. Furthermore, we show that CCDC61 binds microtubules and that residues involved in CCDC61 microtubule binding are important for ciliary function in Chlamydomonas. Together, our findings suggest that CCDC61 and SAS6 functionally diverged from a common ancestor while retaining the ability to scaffold the assembly of basal body-associated structures or centrioles, respectively.

PubMed: 32375023
DOI: 10.1016/j.str.2020.04.010

実験手法

X-RAY DIFFRACTION (2.55 Å)