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1e91
From Proteopedia
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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
Page seeded by OCA on Mon Nov 12 16:41:03 2007
