1g88
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S4AFL3ARG515 MUTANT
OverviewOverview
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.
DiseaseDisease
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 StructureAbout this Structure
1G88 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
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