8IMS

Crystal structure of TRAF7 coiled-coil domain

Summary for 8IMS

• Entry DOI: 10.2210/pdb8ims/pdb
• Descriptor: E3 ubiquitin-protein ligase TRAF7 (2 entities in total)
• Functional Keywords: trimer, e3 ubiquitin-protein ligase, tumor suppressor, signaling protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 3
• Total formula weight: 42287.29

Authors

Hu, R.,Lin, L.,Lu, Q. (deposition date: 2023-03-07, release date: 2024-01-24, Last modification date: 2024-07-17)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.3 Å)