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1khx

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[[Image:1khx.jpg|left|200px]]
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{{Structure
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|RELATEDENTRY=[[1dev|1DEV]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1khx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1khx OCA], [http://www.ebi.ac.uk/pdbsum/1khx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1khx RCSB]</span>
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'''Crystal structure of a phosphorylated Smad2'''
'''Crystal structure of a phosphorylated Smad2'''
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[[Category: Shi, Y.]]
[[Category: Shi, Y.]]
[[Category: Wu, J W.]]
[[Category: Wu, J W.]]
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[[Category: cancer]]
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[[Category: Cancer]]
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[[Category: phosphorylation]]
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[[Category: Phosphorylation]]
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[[Category: receptor kinase signaling]]
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[[Category: Receptor kinase signaling]]
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[[Category: smad2]]
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[[Category: Smad2]]
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[[Category: tgf-beta signaling]]
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[[Category: Tgf-beta signaling]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:46:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:48:52 2008''
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Revision as of 19:46, 2 May 2008

Image:1khx.jpg

Template:STRUCTURE 1khx

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 Fri May 2 22:46:03 2008

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