1U7F
Crystal Structure of the phosphorylated Smad3/Smad4 heterotrimeric complex
Summary for 1U7F
Entry DOI | 10.2210/pdb1u7f/pdb |
Related | 1U7V |
Descriptor | Mothers against decapentaplegic homolog 3, Mothers against decapentaplegic homolog 4 (3 entities in total) |
Functional Keywords | smad, tgf-beta, signal transduction, protein complex, phosphorylation, signaling protein |
Biological source | Homo sapiens (human) More |
Cellular location | Cytoplasm: P84022 Q13485 |
Total number of polymer chains | 3 |
Total formula weight | 70995.24 |
Authors | Chacko, B.M.,Qin, B.Y.,Tiwari, A.,Shi, G.,Lam, S.,Hayward, L.J.,de Caestecker, M.,Lin, K. (deposition date: 2004-08-03, release date: 2004-09-28, Last modification date: 2024-11-20) |
Primary citation | 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 Cited by 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: 15350224DOI: 10.1016/j.molcel.2004.07.016 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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