5YJG

Structural insights into periostin functions

5YJG の概要

• エントリーDOI: 10.2210/pdb5yjg/pdb
• 分子名称: Periostin, SODIUM ION, CYSTEINE, ... (8 entities in total)
• 機能のキーワード: tissue regeneration, cell adhesion
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 71020.60

構造登録者

Liu, H.,Liu, J.,Xu, F. (登録日: 2017-10-10, 公開日: 2018-05-23, 最終更新日: 2024-11-13)

主引用文献

Liu, J.,Zhang, J.,Xu, F.,Lin, Z.,Li, Z.,Liu, H.
Structural characterizations of human periostin dimerization and cysteinylation.
FEBS Lett., 592:1789-1803, 2018

PubMed Abstract: Human periostin plays a multifaceted role in remodeling the extracellular matrix milieu by interacting with other proteins and itself in both a heterophilic and homophilic manner. However, the structural mechanism for its extensive interactions has remained elusive. Here, we report the crystal structures of human periostin (EMI-Fas1 ) and its Cys60Ala mutant. In combination with multi-angle light-scattering analysis and biochemical assays, the crystal structures reveal that periostin mainly exists as a dimer in solution and its homophilic interaction is mainly mediated by the EMI domain. Furthermore, Cys60 undergoes cysteinylation as confirmed by mass spectroscopy, and this site hardly affects the homophilic interaction. Also, the structures yield insights into how periostin forms heterophilic interactions with other proteins under physiological or pathological conditions.

PubMed: 29754429
DOI: 10.1002/1873-3468.13091

実験手法

X-RAY DIFFRACTION (2.399 Å)