1mjs: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /> <applet load="1mjs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mjs, resolution 1.91Å" /> '''MH2 domain of trans...
 
No edit summary
Line 1: Line 1:
[[Image:1mjs.gif|left|200px]]<br />
[[Image:1mjs.gif|left|200px]]<br /><applet load="1mjs" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1mjs" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1mjs, resolution 1.91&Aring;" />
caption="1mjs, resolution 1.91&Aring;" />
'''MH2 domain of transcriptional factor SMAD3'''<br />
'''MH2 domain of transcriptional factor SMAD3'''<br />


==Overview==
==Overview==
Smad3 transduces the signals of TGF-betas, coupling transmembrane receptor, kinase activation to transcriptional control. The membrane-associated, molecule SARA (Smad Anchor for Receptor Activation) recruits Smad3 for, phosphorylation by the receptor kinase. Upon phosphorylation, Smad3, dissociates from SARA and enters the nucleus, in which its transcriptional, activity can be repressed by Ski. Here, we show that SARA and Ski, recognize specifically the monomeric and trimeric forms of Smad3, respectively. Thus, trimerization of Smad3, induced by phosphorylation, simultaneously activates the TGF-beta signal by driving Smad3 dissociation, from SARA and sets up the negative feedback mechanism by Ski. Structural, models of the Smad3/SARA/receptor kinase complex and Smad3/Ski complex, provide insights into the molecular basis of regulation.
Smad3 transduces the signals of TGF-betas, coupling transmembrane receptor kinase activation to transcriptional control. The membrane-associated molecule SARA (Smad Anchor for Receptor Activation) recruits Smad3 for phosphorylation by the receptor kinase. Upon phosphorylation, Smad3 dissociates from SARA and enters the nucleus, in which its transcriptional activity can be repressed by Ski. Here, we show that SARA and Ski recognize specifically the monomeric and trimeric forms of Smad3, respectively. Thus, trimerization of Smad3, induced by phosphorylation, simultaneously activates the TGF-beta signal by driving Smad3 dissociation from SARA and sets up the negative feedback mechanism by Ski. Structural models of the Smad3/SARA/receptor kinase complex and Smad3/Ski complex provide insights into the molecular basis of regulation.


==About this Structure==
==About this Structure==
1MJS 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MJS OCA].  
1MJS 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=1MJS OCA].  


==Reference==
==Reference==
Line 14: Line 13:
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Correia, J.J.]]
[[Category: Correia, J J.]]
[[Category: Lam, S.S.]]
[[Category: Lam, S S.]]
[[Category: Lin, K.]]
[[Category: Lin, K.]]
[[Category: Qin, B.Y.]]
[[Category: Qin, B Y.]]
[[Category: beta sandwich]]
[[Category: beta sandwich]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:12:12 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:55:51 2008''

Revision as of 14:55, 21 February 2008

File:1mjs.gif


1mjs, resolution 1.91Å

Drag the structure with the mouse to rotate

MH2 domain of transcriptional factor SMAD3

OverviewOverview

Smad3 transduces the signals of TGF-betas, coupling transmembrane receptor kinase activation to transcriptional control. The membrane-associated molecule SARA (Smad Anchor for Receptor Activation) recruits Smad3 for phosphorylation by the receptor kinase. Upon phosphorylation, Smad3 dissociates from SARA and enters the nucleus, in which its transcriptional activity can be repressed by Ski. Here, we show that SARA and Ski recognize specifically the monomeric and trimeric forms of Smad3, respectively. Thus, trimerization of Smad3, induced by phosphorylation, simultaneously activates the TGF-beta signal by driving Smad3 dissociation from SARA and sets up the negative feedback mechanism by Ski. Structural models of the Smad3/SARA/receptor kinase complex and Smad3/Ski complex provide insights into the molecular basis of regulation.

About this StructureAbout this Structure

1MJS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Smad3 allostery links TGF-beta receptor kinase activation to transcriptional control., Qin BY, Lam SS, Correia JJ, Lin K, Genes Dev. 2002 Aug 1;16(15):1950-63. PMID:12154125

Page seeded by OCA on Thu Feb 21 13:55:51 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA