1G88

S4AFL3ARG515 MUTANT

1G88 の概要

• エントリーDOI: 10.2210/pdb1g88/pdb
• 関連するPDBエントリー: 1DD1
• 分子名称: SMAD4 (1 entity in total)
• 機能のキーワード: transcriptional factor, l3 loop mutant, transcription
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q13485
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 88045.00

構造登録者

Chako, B.M.,Qin, B.,Lam, S.S.,Correia, J.J.,Lin, K. (登録日: 2000-11-16, 公開日: 2000-11-29, 最終更新日: 2024-02-07)

主引用文献

Chacko, B.M.,Qin, B.,Correia, J.J.,Lam, S.S.,de Caestecker, M.P.,Lin, K.
The L3 loop and C-terminal phosphorylation jointly define Smad protein trimerization.
Nat.Struct.Biol., 8:248-253, 2001

PubMed Abstract: Smad proteins mediate the transforming growth factor beta responses. C-terminal phosphorylation of R-Smads leads to the recruitment of Smad4 and the formation of active signaling complexes. We investigated the mechanism of phosphorylation-induced Smad complex formation with an activating pseudo-phosphorylated Smad3. Pseudo-phosphorylated Smad3 has a greater propensity to homotrimerize, and recruits Smad4 to form a heterotrimer containing two Smad3 and one Smad4. The trimeric interaction is mediated through conserved interfaces to which tumorigenic mutations map. Furthermore, a conserved Arg residue within the L3 loop, located near the C-terminal phosphorylation sites of the neighboring subunit, is essential for trimerization. We propose that the phosphorylated C-terminal residues interact with the L3 loop of the neighboring subunit to stabilize the trimer interaction.

PubMed: 11224571
DOI: 10.1038/84995

実験手法

X-RAY DIFFRACTION (3 Å)