1mk2: Difference between revisions

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|PDB= 1mk2 |SIZE=350|CAPTION= <scene name='initialview01'>1mk2</scene>, resolution 2.74&Aring;
|PDB= 1mk2 |SIZE=350|CAPTION= <scene name='initialview01'>1mk2</scene>, resolution 2.74&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene>
|LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>
|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=[[1mjs|1MJS]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mk2 OCA], [http://www.ebi.ac.uk/pdbsum/1mk2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mk2 RCSB]</span>
}}
}}


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==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.
==Disease==
Known diseases associated with this structure: Anderson disease OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=607690 607690]], Chylomicron retention disease OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=607690 607690]], Mowat-Wilson syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=605802 605802]]


==About this Structure==
==About this Structure==
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[[Category: Lin, K.]]
[[Category: Lin, K.]]
[[Category: Qin, B Y.]]
[[Category: Qin, B Y.]]
[[Category: ACY]]
[[Category: sara]]
[[Category: sara]]
[[Category: sbd]]
[[Category: sbd]]
[[Category: smad3]]
[[Category: smad3]]


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