The Mad1–Sin3B interaction involves a novel helical fold View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2000-12-01

AUTHORS

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

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. More... »

PAGES

nsb1200_1100

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/81944

DOI

http://dx.doi.org/10.1038/81944

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1034228697

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11101889


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