1mhd: Difference between revisions

Line 1:

[[Image:1mhd.gif|left|200px]]<br />

[[Image:1mhd.gif|left|200px]]<br /><applet load="1mhd" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1mhd" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1mhd, resolution 2.8Å" />

'''CRYSTAL STRUCTURE OF A SMAD MH1 DOMAIN BOUND TO DNA'''<br />

==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.

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 [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].

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==

Line 20:

Line 19:

[[Category: smad3 mh1]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 18~~:11:~~13 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:55:09 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1mhd.gif|left|200px]]<br />
+[[Image:1mhd.gif|left|200px]]<br /><applet load="1mhd" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1mhd" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1mhd, resolution 2.8&Aring;" />
 '''CRYSTAL STRUCTURE OF A SMAD MH1 DOMAIN BOUND TO DNA'''<br />
 ==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.
+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==
-MHD 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].
+MHD 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==
@@ Line 20: / Line 19: @@
 [[Category: smad3 mh1]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:11:13 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:55:09 2008''