1e91

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[[Image:1e91.gif|left|200px]]<br /><applet load="1e91" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1e91.gif|left|200px]]
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caption="1e91" />
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'''STRUCTURE OF THE COMPLEX OF THE MAD1-SIN3B INTERACTION DOMAINS'''<br />
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{{Structure
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|PDB= 1e91 |SIZE=350|CAPTION= <scene name='initialview01'>1e91</scene>
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE= SIN3B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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}}
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'''STRUCTURE OF THE COMPLEX OF THE MAD1-SIN3B INTERACTION DOMAINS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1E91 is a [[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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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11101889 11101889]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11101889 11101889]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: eukaryotic transcriptional regulation]]
[[Category: eukaryotic transcriptional regulation]]
[[Category: mad1]]
[[Category: mad1]]
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[[Category: pah domains]]
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[[Category: pah domain]]
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[[Category: protein-protein interactions]]
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[[Category: protein-protein interaction]]
[[Category: sin3]]
[[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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:51:53 2008''

Revision as of 08:51, 20 March 2008


PDB ID 1e91

Drag the structure with the mouse to rotate
Gene: SIN3B (Mus musculus)
Coordinates: save as pdb, mmCIF, xml



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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