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1u7v

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[[Image:1u7v.jpg|left|200px]]
[[Image:1u7v.jpg|left|200px]]
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{{Structure
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|PDB= 1u7v |SIZE=350|CAPTION= <scene name='initialview01'>1u7v</scene>, resolution 2.7&Aring;
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The line below this paragraph, containing "STRUCTURE_1u7v", creates the "Structure Box" on the page.
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|SITE=
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|GENE= SMAD2, MADH2, MADR2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), SMAD4, MADH4, DPC4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_1u7v| PDB=1u7v | SCENE= }}
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|RELATEDENTRY=[[1u7f|1U7F]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u7v OCA], [http://www.ebi.ac.uk/pdbsum/1u7v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u7v RCSB]</span>
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'''Crystal Structure of the phosphorylated Smad2/Smad4 heterotrimeric complex'''
'''Crystal Structure of the phosphorylated Smad2/Smad4 heterotrimeric complex'''
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[[Category: Shi, G.]]
[[Category: Shi, G.]]
[[Category: Tiwari, A.]]
[[Category: Tiwari, A.]]
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[[Category: phosphorylation]]
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[[Category: Phosphorylation]]
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[[Category: protein complex]]
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[[Category: Protein complex]]
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[[Category: signal transduction]]
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[[Category: Signal transduction]]
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[[Category: smad]]
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[[Category: Smad]]
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[[Category: tgf-beta]]
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[[Category: Tgf-beta]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:52:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:06:31 2008''
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Revision as of 07:52, 3 May 2008

Template:STRUCTURE 1u7v

Crystal Structure of the phosphorylated Smad2/Smad4 heterotrimeric complex


Overview

The formation of protein complexes between phosphorylated R-Smads and Smad4 is a central event in the TGF-beta signaling pathway. We have determined the crystal structure of two R-Smad/Smad4 complexes, Smad3/Smad4 to 2.5 angstroms, and Smad2/Smad4 to 2.7 angstroms. Both complexes are heterotrimers, comprising two phosphorylated R-Smad subunits and one Smad4 subunit, a finding that was corroborated by isothermal titration calorimetry and mutational studies. Preferential formation of the R-Smad/Smad4 heterotrimer over the R-Smad homotrimer is largely enthalpy driven, contributed by the unique presence of strong electrostatic interactions within the heterotrimeric interfaces. The study supports a common mechanism of Smad protein assembly in TGF-beta superfamily signaling.

About this Structure

1U7V is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis of heteromeric smad protein assembly in TGF-beta signaling., Chacko BM, Qin BY, Tiwari A, Shi G, Lam S, Hayward LJ, De Caestecker M, Lin K, Mol Cell. 2004 Sep 10;15(5):813-23. PMID:15350224 Page seeded by OCA on Sat May 3 10:52:06 2008

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