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1u7f
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(New page: 200px<br /> <applet load="1u7f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u7f, resolution 2.6Å" /> '''Crystal Structure of...)
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Revision as of 17:26, 12 November 2007
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Crystal Structure of the phosphorylated Smad3/Smad4 heterotrimeric complex
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Juvenile polyposis/hereditary hemorrhagic telangiectasia syndrome OMIM:[600993], Pancreatic cancer OMIM:[600993], Polyposis, juvenile intestinal OMIM:[600993]
About this Structure
1U7F is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis of heteromeric smad protein assembly in TGF-beta signaling., Chacko BM, Qin BY, Tiwari A, Shi G, Lam S, Hayward LJ, De Caestecker M, Lin K, Mol Cell. 2004 Sep 10;15(5):813-23. PMID:15350224
Page seeded by OCA on Mon Nov 12 19:32:27 2007
