1khx

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{{STRUCTURE_1khx| PDB=1khx | SCENE= }}
{{STRUCTURE_1khx| PDB=1khx | SCENE= }}
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'''Crystal structure of a phosphorylated Smad2'''
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===Crystal structure of a phosphorylated Smad2===
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==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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11779503 is the PubMed ID number.
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:22:15 2008''

Revision as of 07:22, 2 July 2008

Image:1khx.png

Template:STRUCTURE 1khx

Crystal structure of a phosphorylated Smad2

Template:ABSTRACT PUBMED 11779503

About this Structure

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

Reference

Crystal structure of a phosphorylated Smad2. Recognition of phosphoserine by the MH2 domain and insights on Smad function in TGF-beta signaling., Wu JW, Hu M, Chai J, Seoane J, Huse M, Li C, Rigotti DJ, Kyin S, Muir TW, Fairman R, Massague J, Shi Y, Mol Cell. 2001 Dec;8(6):1277-89. PMID:11779503

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