1g88

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{{STRUCTURE_1g88| PDB=1g88 | SCENE= }}
{{STRUCTURE_1g88| PDB=1g88 | SCENE= }}
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'''S4AFL3ARG515 MUTANT'''
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===S4AFL3ARG515 MUTANT===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_11224571}}
==About this Structure==
==About this Structure==
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[[Category: L3 loop mutant]]
[[Category: L3 loop mutant]]
[[Category: Transcriptional factor]]
[[Category: Transcriptional factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:16:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:52:14 2008''

Revision as of 01:52, 1 July 2008

Image:1g88.png

Template:STRUCTURE 1g88

S4AFL3ARG515 MUTANT

Template:ABSTRACT PUBMED 11224571

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

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