1khx
From Proteopedia
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- | [[Image:1khx.jpg|left|200px]] | + | [[Image:1khx.jpg|left|200px]] |
- | + | ||
- | '''Crystal structure of a phosphorylated Smad2''' | + | {{Structure |
+ | |PDB= 1khx |SIZE=350|CAPTION= <scene name='initialview01'>1khx</scene>, resolution 1.8Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''Crystal structure of a phosphorylated Smad2''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1KHX is a [ | + | 1KHX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KHX OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11779503 11779503] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tgf-beta signaling]] | [[Category: tgf-beta signaling]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:17:42 2008'' |
Revision as of 10:17, 20 March 2008
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, resolution 1.8Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
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 Mar 20 12:17:42 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