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1mr1

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This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

1mr1, resolution 2.85Å ()

Ligands:

Domains:

MH2, c-SKI_SMAD_bind

Related:

1ygs

Structural annotation:
Resources:	CATH : 1Mr1A00, 1Mr1B00, 1Mr1C00, 1Mr1D00 InterPro : Ipr003619, Ipr001132, Ipr008984, Ipr013790, Ipr013019, Ipr009061, Ipr014890, Ipr010919, Ipr003380 Pfam : PF03166, PF08782 SCOP : d1mr1a_, d1mr1b_, d1mr1c_, d1mr1d_ UniProt : Q13485, P12755

Functional annotation:
Resources:	GeneCard : SMAD4, SKI
Cellular component:	intracellular cytoplasm transcription factor complex nucleus transcriptional repressor complex
Biological process:	ureteric bud branching positive regulation of transcription from RNA polymerase II promoter regulation of transcription from RNA polymerase II promoter regulation of binding positive regulation of transcription, DNA-dependent SMAD protein complex assembly transforming growth factor beta receptor signaling pathway kidney development negative regulation of cell proliferation transcription regulation of transcription, DNA-dependent anterior/posterior pattern formation embryonic limb morphogenesis cell differentiation
Molecular function:	transcription activator activity protein binding DNA binding transcription factor activity transcription cofactor activity binding nucleotide binding molecular_function

Evolutionary conservation:

Toggle Conservation Colors:

Rows = identical sequences:

Further Information:

Caveats,

Explanation,
Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

Crystal Structure of a Smad4-Ski Complex

Publication Abstract from PubMed

The Ski family of nuclear oncoproteins represses TGF-beta signaling through interactions with the Smad proteins. The crystal structure of the Smad4 binding domain of human c-Ski in complex with the MH2 domain of Smad4 reveals specific recognition of the Smad4 L3 loop region by a highly conserved interaction loop (I loop) from Ski. The Ski binding surface on Smad4 significantly overlaps with that required for binding of the R-Smads. Indeed, Ski disrupts the formation of a functional complex between the Co- and R-Smads, explaining how it could lead to repression of TGF-beta, activin, and BMP responses. Intriguingly, the structure of the Ski fragment, stabilized by a bound zinc atom, resembles the SAND domain, in which the corresponding I loop is responsible for DNA binding.

Structural mechanism of Smad4 recognition by the nuclear oncoprotein Ski: insights on Ski-mediated repression of TGF-beta signaling., Wu JW, Krawitz AR, Chai J, Li W, Zhang F, Luo K, Shi Y, Cell. 2002 Nov 1;111(3):357-67. PMID:12419246

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1MR1 is a 4 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Wu JW, Krawitz AR, Chai J, Li W, Zhang F, Luo K, Shi Y. Structural mechanism of Smad4 recognition by the nuclear oncoprotein Ski: insights on Ski-mediated repression of TGF-beta signaling. Cell. 2002 Nov 1;111(3):357-67. PMID:12419246

Page seeded by OCA on Tue Feb 17 10:41:52 2009

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1mr1

From Proteopedia

Crystal Structure of a Smad4-Ski Complex

About this Structure

Reference

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