The Mad1-Sin3B interaction involves a novel helical fold

Christian A.E.M. Spronk, Marco Tessari, Anita M. Kaan, Jacobus F.A. Jansen, Michiel Vermeulen, Hendrik G. Stunnenberg, Geerten W. Vuister

Onderzoeksoutput: Bijdrage aan tijdschriftArtikelpeer review

52 Citaten (Scopus)


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 α-helices of PAH2 form a hydrophobic cleft that accommodates an amphipathic Mad1 α-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.

Originele taal-2Engels
Pagina's (van-tot)1100-1104
Aantal pagina's5
TijdschriftNature Structural Biology
Nummer van het tijdschrift12
StatusGepubliceerd - 2000
Extern gepubliceerdJa


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