1g88
From Proteopedia
(New page: 200px<br /> <applet load="1g88" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g88, resolution 3.00Å" /> '''S4AFL3ARG515 MUTANT...) |
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| - | [[Image:1g88.gif|left|200px]]<br /> | + | [[Image:1g88.gif|left|200px]]<br /><applet load="1g88" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1g88" size=" | + | |
caption="1g88, resolution 3.00Å" /> | caption="1g88, resolution 3.00Å" /> | ||
'''S4AFL3ARG515 MUTANT'''<br /> | '''S4AFL3ARG515 MUTANT'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Smad proteins mediate the transforming growth factor beta responses. | + | 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. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1G88 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1G88 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G88 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chako, B | + | [[Category: Chako, B M.]] |
| - | [[Category: Correia, J | + | [[Category: Correia, J J.]] |
| - | [[Category: Lam, S | + | [[Category: Lam, S S.]] |
[[Category: Lin, K.]] | [[Category: Lin, K.]] | ||
[[Category: Qin, B.]] | [[Category: Qin, B.]] | ||
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[[Category: transcriptional factor]] | [[Category: transcriptional factor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:47:12 2008'' |
Revision as of 10:47, 21 February 2008
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S4AFL3ARG515 MUTANT
Contents |
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.
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
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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