First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.
1g88
From Proteopedia
S4AFL3ARG515 MUTANT
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.
The L3 loop and C-terminal phosphorylation jointly define Smad protein trimerization., Chacko BM, Qin B, Correia JJ, Lam SS, de Caestecker MP, Lin K, Nat Struct Biol. 2001 Mar;8(3):248-53. PMID:11224571
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1G88 is a 3 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Chacko BM, Qin B, Correia JJ, Lam SS, de Caestecker MP, Lin K. The L3 loop and C-terminal phosphorylation jointly define Smad protein trimerization. Nat Struct Biol. 2001 Mar;8(3):248-53. PMID:11224571 doi:10.1038/84995
Page seeded by OCA on Wed Feb 18 02:56:47 2009
