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1g88
From Proteopedia
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[[Image:1g88.gif|left|200px]] | [[Image:1g88.gif|left|200px]] | ||
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'''S4AFL3ARG515 MUTANT''' | '''S4AFL3ARG515 MUTANT''' | ||
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[[Category: Lin, K.]] | [[Category: Lin, K.]] | ||
[[Category: Qin, B.]] | [[Category: Qin, B.]] | ||
| - | [[Category: | + | [[Category: L3 loop mutant]] |
| - | [[Category: | + | [[Category: Transcriptional factor]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:16:01 2008'' | |
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Revision as of 14:16, 2 May 2008
S4AFL3ARG515 MUTANT
Overview
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.
About this Structure
1G88 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 17:16:01 2008
