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1khx
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Ligand-induced phosphorylation of the receptor-regulated Smads (R-Smads) | + | 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== | ==About this Structure== | ||
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[[Category: Kyin, S.]] | [[Category: Kyin, S.]] | ||
[[Category: Massague, J.]] | [[Category: Massague, J.]] | ||
| - | [[Category: Muir, T | + | [[Category: Muir, T W.]] |
[[Category: Seoane, J.]] | [[Category: Seoane, J.]] | ||
[[Category: Shi, Y.]] | [[Category: Shi, Y.]] | ||
| - | [[Category: Wu, J | + | [[Category: Wu, J W.]] |
[[Category: cancer]] | [[Category: cancer]] | ||
[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
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[[Category: tgf-beta signaling]] | [[Category: tgf-beta signaling]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:34:24 2008'' |
Revision as of 11:34, 21 February 2008
|
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
Page seeded by OCA on Thu Feb 21 13:34:24 2008
Categories: Homo sapiens | Single protein | Chai, J. | Fairman, R. | Hu, M. | Huse, M. | Kyin, S. | Massague, J. | Muir, T W. | Seoane, J. | Shi, Y. | Wu, J W. | Cancer | Phosphorylation | Receptor kinase signaling | Smad2 | Tgf-beta signaling
