1khx: Difference between revisions

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[[Image:1khx.jpg|left|200px]]
{{Seed}}
[[Image:1khx.png|left|200px]]


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{{STRUCTURE_1khx|  PDB=1khx  |  SCENE=  }}  
{{STRUCTURE_1khx|  PDB=1khx  |  SCENE=  }}  


'''Crystal structure of a phosphorylated Smad2'''
===Crystal structure of a phosphorylated Smad2===




==Overview==
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Ligand-induced phosphorylation of the receptor-regulated Smads (R-Smads) is essential in the receptor Ser/Thr kinase-mediated TGF-beta signaling. The crystal structure of a phosphorylated Smad2, at 1.8 A resolution, reveals the formation of a homotrimer mediated by the C-terminal phosphoserine (pSer) residues. The pSer binding surface on the MH2 domain, frequently targeted for inactivation in cancers, is highly conserved among the Co- and R-Smads. This finding, together with mutagenesis data, pinpoints a functional interface between Smad2 and Smad4. In addition, the pSer binding surface on the MH2 domain coincides with the surface on R-Smads that is required for docking interactions with the serine-phosphorylated receptor kinases. These observations define a bifunctional role for the MH2 domain as a pSer-X-pSer binding module in receptor Ser/Thr kinase signaling pathways.
The line below this paragraph, {{ABSTRACT_PUBMED_11779503}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_11779503}}


==About this Structure==
==About this Structure==
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[[Category: Smad2]]
[[Category: Smad2]]
[[Category: Tgf-beta signaling]]
[[Category: Tgf-beta signaling]]
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