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1e91
From Proteopedia
(New page: 200px<br /> <applet load="1e91" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e91" /> '''STRUCTURE OF THE COMPLEX OF THE MAD1-SIN3B ...) |
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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=" | + | |
caption="1e91" /> | caption="1e91" /> | ||
'''STRUCTURE OF THE COMPLEX OF THE MAD1-SIN3B INTERACTION DOMAINS'''<br /> | '''STRUCTURE OF THE COMPLEX OF THE MAD1-SIN3B INTERACTION DOMAINS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Sin3A or Sin3B are components of a corepressor complex that mediates | + | 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== | ==Disease== | ||
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==About this Structure== | ==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:// | + | 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== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Jansen, J | + | [[Category: Jansen, J F.A.]] |
| - | [[Category: Kaan, A | + | [[Category: Kaan, A M.]] |
| - | [[Category: Spronk, C | + | [[Category: Spronk, C A.E M.]] |
| - | [[Category: Stunnenberg, H | + | [[Category: Stunnenberg, H G.]] |
[[Category: Tessari, M.]] | [[Category: Tessari, M.]] | ||
[[Category: Vermeulen, M.]] | [[Category: Vermeulen, M.]] | ||
| - | [[Category: Vuister, G | + | [[Category: Vuister, G W.]] |
[[Category: eukaryotic transcriptional regulation]] | [[Category: eukaryotic transcriptional regulation]] | ||
[[Category: mad1]] | [[Category: mad1]] | ||
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[[Category: sin3]] | [[Category: sin3]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:25:10 2008'' |
Revision as of 10:25, 21 February 2008
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STRUCTURE OF THE COMPLEX OF THE MAD1-SIN3B INTERACTION DOMAINS
Contents |
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.
Disease
Known diseases associated with this structure: Lymphoma, somatic OMIM:[602686], Prostate cancer, somatic OMIM:[602686]
About this Structure
1E91 is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
Reference
The Mad1-Sin3B interaction involves a novel helical fold., Spronk CA, Tessari M, Kaan AM, Jansen JF, Vermeulen M, Stunnenberg HG, Vuister GW, Nat Struct Biol. 2000 Dec;7(12):1100-4. PMID:11101889
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