1mhd
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(New page: 200px<br /> <applet load="1mhd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mhd, resolution 2.8Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 16:04, 12 November 2007
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CRYSTAL STRUCTURE OF A SMAD MH1 DOMAIN BOUND TO DNA
Overview
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.
About this Structure
1MHD is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
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