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Title: The Mad1-Sin3B interaction involves a novel helical fold.
Authors: Spronk, CA
Tessari, M
Kaan, AM
Jansen, JF
Vermeulen, M
Stunnenberg, HG
Vuister, GW
First Published: Dec-2000
Citation: NAT STRUCT BIOL, 2000, 7 (12), pp. 1100-1104
Abstract: 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.
DOI Link: 10.1038/81944
ISSN: 1072-8368
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

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