1E91

Structure of the complex of the Mad1-Sin3B interaction domains

Summary for 1E91

• Entry DOI: 10.2210/pdb1e91/pdb
• NMR Information: BMRB: 4841,5457
• Descriptor: PAIRED AMPHIPATHIC HELIX PROTEIN SIN3B, MAD PROTEIN (MAX DIMERIZER) (2 entities in total)
• Functional Keywords: eukaryotic transcriptional regulation, sin3, pah domains, mad1, protein-protein interactions
• Biological source: MUS MUSCULUS (HOUSE MOUSE); More
• Cellular location: Nucleus : Q62141 Q05195
• Total number of polymer chains: 2
• Total formula weight: 11619.98

Authors

Spronk, C.A.E.M.,Tessari, M.,Kaan, A.M.,Jansen, J.F.A.,Vermeulen, M.,Stunnenberg, H.G.,Vuister, G.W. (deposition date: 2000-10-04, release date: 2000-11-20, Last modification date: 2024-05-15)

Primary citation

Spronk, C.A.E.M.,Tessari, M.,Kaan, A.M.,Jansen, J.F.A.,Vermeulen, M.,Stunnenberg, H.G.,Vuister, G.W.
The MAD1-Sin3B Interaction Involves a Novel Helical Fold
Nat.Struct.Biol., 7:1100-1104, 2000

PubMed 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.

PubMed: 11101889
DOI: 10.1038/81944

Experimental method

SOLUTION NMR