[HTML][HTML] Crystal structure of a Smad MH1 domain bound to DNA: insights on DNA binding in TGF-β signaling
Y Shi, YF Wang, L Jayaraman, H Yang, J Massagué… - Cell, 1998 - cell.com
Y Shi, YF Wang, L Jayaraman, H Yang, J Massagué, NP Pavletich
Cell, 1998•cell.comThe Smad family of proteins, which are frequently targeted by tumorigenic mutations in
cancer, mediate TGF-β signaling from cell membrane to nucleus. The crystal structure of a
Smad3 MH1 domain bound to an optimal DNA sequence determined at 2.8 Å resolution
reveals a novel DNA-binding motif. In the crystals, base-specific DNA recognition is provided
exclusively by a conserved 11-residue β hairpin that is embedded in the major groove of
DNA. A surface loop region, to which tumorigenic mutations map, has been identified as a …
cancer, mediate TGF-β signaling from cell membrane to nucleus. The crystal structure of a
Smad3 MH1 domain bound to an optimal DNA sequence determined at 2.8 Å resolution
reveals a novel DNA-binding motif. In the crystals, base-specific DNA recognition is provided
exclusively by a conserved 11-residue β hairpin that is embedded in the major groove of
DNA. A surface loop region, to which tumorigenic mutations map, has been identified as a …
Abstract
The Smad family of proteins, which are frequently targeted by tumorigenic mutations in cancer, mediate TGF-β signaling from cell membrane to nucleus. The crystal structure of a Smad3 MH1 domain bound to an optimal DNA sequence determined at 2.8 Å resolution reveals a novel DNA-binding motif. In the crystals, base-specific DNA recognition is provided exclusively by a conserved 11-residue β 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-β-responsive genes.
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