8IMS

Crystal structure of TRAF7 coiled-coil domain

8IMS の概要

• エントリーDOI: 10.2210/pdb8ims/pdb
• 分子名称: E3 ubiquitin-protein ligase TRAF7 (2 entities in total)
• 機能のキーワード: trimer, e3 ubiquitin-protein ligase, tumor suppressor, signaling 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: 42287.29

構造登録者

Hu, R.,Lin, L.,Lu, Q. (登録日: 2023-03-07, 公開日: 2024-01-24, 最終更新日: 2024-07-17)

主引用文献

Song, X.,Hu, R.,Chen, Y.,Xiao, M.,Zhang, H.,Wu, S.,Lu, Q.
The structure of TRAF7 coiled-coil trimer provides insight into its function in zebrafish embryonic development.
J Mol Cell Biol, 16:-, 2024

PubMed Abstract: TRAF7 serves as a crucial intracellular adaptor and E3 ubiquitin ligase involved in signal transduction pathways, contributing to immune responses, tumor progression, and embryonic development. Somatic mutations within the coiled-coil (CC) domain and WD40 repeat domain of TRAF7 could cause brain tumors, while germline pathogenic mutations contribute to severe developmental abnormalities. However, the precise molecular mechanism underlying TRAF7 involvement in embryonic development remains unclear. In this study, we employed zebrafish as an in vivo model system. TRAF7 knock down caused defects in zebrafish embryonic development. We determined the crystal structure of TRAF7 CC domain at 3.3 Å resolution and found that the CC region trimerization was essential for TRAF7 functionality during zebrafish embryonic development. Additionally, disease-causing mutations in TRAF7 CC region could impair the trimer formation, consequently impacting early embryonic development of zebrafish. Therefore, our study sheds light on the molecular mechanism of TRAF7 CC trimer formation and its pivotal role in embryonic development.

PubMed: 38178633
DOI: 10.1093/jmcb/mjad083

実験手法

X-RAY DIFFRACTION (3.3 Å)