1khx

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spinqualitylabelsall models 1khx, resolution 1.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of a phosphorylated Smad2

Overview

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.

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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