5Y4D

Crystal Structure of AnkB Ankyrin Repeats in Complex with AnkR/AnkB Chimeric Autoinhibition Segment

5Y4D の概要

• エントリーDOI: 10.2210/pdb5y4d/pdb
• 分子名称: Ankyrin-1,Ankyrin-2,Ankyrin-2, SULFATE ION (2 entities in total)
• 機能のキーワード: ank repeat, protein-protein interaction, structural protein, auto-inhibition, protein binding
• 由来する生物種: Mus musculus (Mouse); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton : Q01484
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 78987.55

構造登録者

Chen, K.,Li, J.,Wang, C.,Wei, Z.,Zhang, M. (登録日: 2017-08-03, 公開日: 2017-09-13, 最終更新日: 2025-09-17)

主引用文献

Chen, K.,Li, J.,Wang, C.,Wei, Z.,Zhang, M.
Autoinhibition of ankyrin-B/G membrane target bindings by intrinsically disordered segments from the tail regions.
Elife, 6:-, 2017

PubMed Abstract: Ankyrins together with their spectrin partners are the master organizers of micron-scale membrane domains in diverse tissues. The 24 ankyrin (ANK) repeats of ankyrins bind to numerous membrane proteins, linking them to spectrin-based cytoskeletons at specific membrane microdomains. The accessibility of the target binding groove of ANK repeats must be regulated to achieve spatially defined functions of ankyrins/target complexes in different tissues, though little is known in this regard. Here we systemically investigated the autoinhibition mechanism of ankyrin-B/G by combined biochemical, biophysical and structural biology approaches. We discovered that the entire ANK repeats are inhibited by combinatorial and quasi-independent bindings of multiple disordered segments located in the ankyrin-B/G linkers and tails, suggesting a mechanistic basis for differential regulations of membrane target bindings by ankyrins. In addition to elucidating the autoinhibition mechanisms of ankyrins, our study may also shed light on regulations on target bindings by other long repeat-containing proteins.

PubMed: 28841137
DOI: 10.7554/eLife.29150

実験手法

X-RAY DIFFRACTION (3.3 Å)