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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 2.8&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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<applet load="1mhd" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1mhd, resolution 2.8&Aring;" />
'''CRYSTAL STRUCTURE OF A SMAD MH1 DOMAIN BOUND TO DNA'''<br />
'''CRYSTAL STRUCTURE OF A SMAD MH1 DOMAIN BOUND TO DNA'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1MHD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MHD OCA].
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1MHD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MHD OCA].
==Reference==
==Reference==
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[[Category: smad3 mh1]]
[[Category: smad3 mh1]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:11:13 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:55:09 2008''

Revision as of 11:55, 21 February 2008


1mhd, resolution 2.8Å

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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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