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1mhd

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1mhd, resolution 2.80Å ()

Gene:

SMAD (Homo sapiens)

Domains:

MH1

Structural annotation:
Resources:	CATH : 1Mhda00, 1Mhdb00 InterPro : Ipr001132, Ipr013790, Ipr008984, Ipr003619, Ipr013019 Pfam : PF03165 SCOP : d1mhda_, d1mhdb_ UniProt : P84022

Functional annotation:
Resources:	GeneCard : SMAD3
Cellular component:	plasma membrane intracellular nucleus cytoplasm
Biological process:	regulation of striated muscle development negative regulation of transcription from RNA polymerase II promoter positive regulation of transcription positive regulation of transcription, DNA-dependent regulation of epithelial cell proliferation transcription regulation of binding paraxial mesoderm morphogenesis regulation of transcription, DNA-dependent mesoderm formation transcription from RNA polymerase II promoter T cell activation transforming growth factor beta receptor signaling pathway regulation of transforming growth factor beta receptor signaling pathway positive regulation of transcription from RNA polymerase II promoter regulation of immune response
Molecular function:	transcription factor activity transcription factor binding transcription activator activity protein binding double-stranded DNA binding

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 SMAD MH1 DOMAIN BOUND TO DNA

Publication Abstract from PubMed

The Smad family of proteins, which are frequently targeted by tumorigenic mutations in cancer, mediate TGF-beta signaling from cell membrane to nucleus. The crystal structure of a Smad3 MH1 domain bound to an optimal DNA sequence determined at 2.8 A resolution reveals a novel DNA-binding motif. In the crystals, base-specific DNA recognition is provided exclusively by a conserved 11-residue beta hairpin that is embedded in the major groove of DNA. A surface loop region, to which tumorigenic mutations map, has been identified as a functional surface important for Smad activity. This structure establishes a framework for understanding how Smad proteins may act in concert with other transcription factors in the regulation of TGF-beta-responsive genes.

Crystal structure of a Smad MH1 domain bound to DNA: insights on DNA binding in TGF-beta signaling., Shi Y, Wang YF, Jayaraman L, Yang H, Massague J, Pavletich NP, Cell. 1998 Sep 4;94(5):585-94. PMID:9741623

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

About this Structure

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

Reference

Shi Y, Wang YF, Jayaraman L, Yang H, Massague J, Pavletich NP. Crystal structure of a Smad MH1 domain bound to DNA: insights on DNA binding in TGF-beta signaling. Cell. 1998 Sep 4;94(5):585-94. PMID:9741623

Page seeded by OCA on Tue Feb 17 18:46:13 2009