1U7F

Crystal Structure of the phosphorylated Smad3/Smad4 heterotrimeric complex

1U7F の概要

• エントリーDOI: 10.2210/pdb1u7f/pdb
• 関連するPDBエントリー: 1U7V
• 分子名称: Mothers against decapentaplegic homolog 3, Mothers against decapentaplegic homolog 4 (3 entities in total)
• 機能のキーワード: smad, tgf-beta, signal transduction, protein complex, phosphorylation, signaling protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: P84022 Q13485
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 70995.24

構造登録者

Chacko, B.M.,Qin, B.Y.,Tiwari, A.,Shi, G.,Lam, S.,Hayward, L.J.,de Caestecker, M.,Lin, K. (登録日: 2004-08-03, 公開日: 2004-09-28, 最終更新日: 2024-11-20)

主引用文献

Chacko, B.M.,Qin, B.Y.,Tiwari, A.,Shi, G.,Lam, S.,Hayward, L.J.,De Caestecker, M.,Lin, K.
Structural basis of heteromeric smad protein assembly in tgf-Beta signaling
Mol.Cell, 15:813-823, 2004

PubMed Abstract: The formation of protein complexes between phosphorylated R-Smads and Smad4 is a central event in the TGF-beta signaling pathway. We have determined the crystal structure of two R-Smad/Smad4 complexes, Smad3/Smad4 to 2.5 angstroms, and Smad2/Smad4 to 2.7 angstroms. Both complexes are heterotrimers, comprising two phosphorylated R-Smad subunits and one Smad4 subunit, a finding that was corroborated by isothermal titration calorimetry and mutational studies. Preferential formation of the R-Smad/Smad4 heterotrimer over the R-Smad homotrimer is largely enthalpy driven, contributed by the unique presence of strong electrostatic interactions within the heterotrimeric interfaces. The study supports a common mechanism of Smad protein assembly in TGF-beta superfamily signaling.

PubMed: 15350224
DOI: 10.1016/j.molcel.2004.07.016

実験手法

X-RAY DIFFRACTION (2.6 Å)