5XME

Solution structure of C-terminal domain of TRADD

5XME の概要

• エントリーDOI: 10.2210/pdb5xme/pdb
• NMR情報: BMRB: 36084
• 分子名称: Tumor necrosis factor receptor type 1-associated DEATH domain protein (1 entity in total)
• 機能のキーワード: tradd, death domain, apoptosis
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Nucleus : Q15628
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14429.22

構造登録者

Lin, Z.,Zhang, N. (登録日: 2017-05-15, 公開日: 2017-09-06, 最終更新日: 2024-05-01)

主引用文献

Zhang, N.,Yuan, W.,Fan, J.S.,Lin, Z.
Structure of the C-terminal domain of TRADD reveals a novel fold in the death domain superfamily.
Sci Rep, 7:7073-7073, 2017

PubMed Abstract: The TNFR1-associated death domain protein (TRADD) is an intracellular adaptor protein involved in various signaling pathways, such as antiapoptosis. Its C-terminal death domain (DD) is responsible for binding other DD-containing proteins including the p75 neurotrophin receptor (p75). Here we present a solution structure of TRADD DD derived from high-resolution NMR spectroscopy. The TRADD DD comprises two super-secondary structures, an all-helix Greek key motif and a β-hairpin motif flanked by two α helices, which make it unique among all known DD structures. The β-hairpin motif is essential for TRADD DD to fold into a functional globular domain. The highly-charged surface suggests a critical role of electrostatic interactions in TRADD DD-mediated signaling. This novel structure represents a new class within the DD superfamily and provides a structural basis for studying homotypic DD interactions. NMR titration revealed a direct weak interaction between TRADD DD and p75 DD monomers. A binding site next to the p75 DD homodimerization interface indicates that TRADD DD recruitment to p75 requires separation of the p75 DD homodimer, explaining the mechanism of NGF-dependent activation of p75-TRADD-mediated antiapoptotic pathway in breast cancer cell.

PubMed: 28765645
DOI: 10.1038/s41598-017-07348-9

実験手法

SOLUTION NMR