1e91: Difference between revisions

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[[Image:1e91.gif|left|200px]]<br />

[[Image:1e91.gif|left|200px]]<br /><applet load="1e91" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1e91" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1e91" />

'''STRUCTURE OF THE COMPLEX OF THE MAD1-SIN3B INTERACTION DOMAINS'''<br />

==Overview==

Sin3A or Sin3B are components of a corepressor complex that mediates, repression by transcription factors such as the helix-loop-helix proteins, Mad and Mxi. Members of the Mad/Mxi family of repressors play important, roles in the transition between proliferation and differentiation by, down-regulating the expression of genes that are activated by the, proto-oncogene product Myc. Here, we report the solution structure of the, second paired amphipathic helix (PAH) domain (PAH2) of Sin3B in complex, with a peptide comprising the N-terminal region of Mad1. This complex, exhibits a novel interaction fold for which we propose the name 'wedged, helical bundle'. Four alpha-helices of PAH2 form a hydrophobic cleft that, accommodates an amphipathic Mad1 alpha-helix. Our data further show that, upon binding Mad1, secondary structure elements of PAH2 are stabilized., The PAH2-Mad1 structure provides the basis for determining the principles, of protein interaction and selectivity involving PAH domains.

Sin3A or Sin3B are components of a corepressor complex that mediates repression by transcription factors such as the helix-loop-helix proteins Mad and Mxi. Members of the Mad/Mxi family of repressors play important roles in the transition between proliferation and differentiation by down-regulating the expression of genes that are activated by the proto-oncogene product Myc. Here, we report the solution structure of the second paired amphipathic helix (PAH) domain (PAH2) of Sin3B in complex with a peptide comprising the N-terminal region of Mad1. This complex exhibits a novel interaction fold for which we propose the name 'wedged helical bundle'. Four alpha-helices of PAH2 form a hydrophobic cleft that accommodates an amphipathic Mad1 alpha-helix. Our data further show that, upon binding Mad1, secondary structure elements of PAH2 are stabilized. The PAH2-Mad1 structure provides the basis for determining the principles of protein interaction and selectivity involving PAH domains.

==Disease==

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==About this Structure==

1E91 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1E91 OCA].

1E91 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E91 OCA].

==Reference==

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[[Category: Mus musculus]]

[[Category: Protein complex]]

[[Category: Jansen, J.F.A.]]

[[Category: Jansen, J F.A.]]

[[Category: Kaan, A.M.]]

[[Category: Kaan, A M.]]

[[Category: Spronk, C.A.E.M.]]

[[Category: Spronk, C A.E M.]]

[[Category: Stunnenberg, H.G.]]

[[Category: Stunnenberg, H G.]]

[[Category: Tessari, M.]]

[[Category: Vermeulen, M.]]

[[Category: Vuister, G.W.]]

[[Category: Vuister, G W.]]

[[Category: eukaryotic transcriptional regulation]]

[[Category: mad1]]

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[[Category: sin3]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:25:10 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1e91.gif|left|200px]]<br />
+[[Image:1e91.gif|left|200px]]<br /><applet load="1e91" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1e91" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1e91" />
 '''STRUCTURE OF THE COMPLEX OF THE MAD1-SIN3B INTERACTION DOMAINS'''<br />
 ==Overview==
-Sin3A or Sin3B are components of a corepressor complex that mediates, repression by transcription factors such as the helix-loop-helix proteins, Mad and Mxi. Members of the Mad/Mxi family of repressors play important, roles in the transition between proliferation and differentiation by, down-regulating the expression of genes that are activated by the, proto-oncogene product Myc. Here, we report the solution structure of the, second paired amphipathic helix (PAH) domain (PAH2) of Sin3B in complex, with a peptide comprising the N-terminal region of Mad1. This complex, exhibits a novel interaction fold for which we propose the name 'wedged, helical bundle'. Four alpha-helices of PAH2 form a hydrophobic cleft that, accommodates an amphipathic Mad1 alpha-helix. Our data further show that, upon binding Mad1, secondary structure elements of PAH2 are stabilized., The PAH2-Mad1 structure provides the basis for determining the principles, of protein interaction and selectivity involving PAH domains.
+Sin3A or Sin3B are components of a corepressor complex that mediates repression by transcription factors such as the helix-loop-helix proteins Mad and Mxi. Members of the Mad/Mxi family of repressors play important roles in the transition between proliferation and differentiation by down-regulating the expression of genes that are activated by the proto-oncogene product Myc. Here, we report the solution structure of the second paired amphipathic helix (PAH) domain (PAH2) of Sin3B in complex with a peptide comprising the N-terminal region of Mad1. This complex exhibits a novel interaction fold for which we propose the name 'wedged helical bundle'. Four alpha-helices of PAH2 form a hydrophobic cleft that accommodates an amphipathic Mad1 alpha-helix. Our data further show that, upon binding Mad1, secondary structure elements of PAH2 are stabilized. The PAH2-Mad1 structure provides the basis for determining the principles of protein interaction and selectivity involving PAH domains.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-E91 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E91 OCA].
+E91 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E91 OCA].
 ==Reference==
@@ Line 18: / Line 17: @@
 [[Category: Mus musculus]]
 [[Category: Protein complex]]
-[[Category: Jansen, J.F.A.]]
+[[Category: Jansen, J F.A.]]
-[[Category: Kaan, A.M.]]
+[[Category: Kaan, A M.]]
-[[Category: Spronk, C.A.E.M.]]
+[[Category: Spronk, C A.E M.]]
-[[Category: Stunnenberg, H.G.]]
+[[Category: Stunnenberg, H G.]]
 [[Category: Tessari, M.]]
 [[Category: Vermeulen, M.]]
-[[Category: Vuister, G.W.]]
+[[Category: Vuister, G W.]]
 [[Category: eukaryotic transcriptional regulation]]
 [[Category: mad1]]
@@ Line 31: / Line 30: @@
 [[Category: sin3]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:41:03 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:25:10 2008''