1PD7

Extended SID of Mad1 bound to the PAH2 domain of mSin3B

Summary for 1PD7

• Entry DOI: 10.2210/pdb1pd7/pdb
• Related: 1E91 1G1E
• NMR Information: BMRB: 5457,5808
• Descriptor: Sin3b protein, Mad1 (2 entities in total)
• Functional Keywords: pah2, sin3, mad1, eukaryotic transcriptional regulation, protein-protein interactions, transcription
• Biological source: Mus musculus (house mouse); More
• Cellular location: Nucleus: Q62141 Q05195
• Total number of polymer chains: 2
• Total formula weight: 13075.65

Authors

Van Ingen, H.,Lasonder, E.,Jansen, J.F.,Kaan, A.M.,Spronk, C.A.,Stunnenberg, H.G.,Vuister, G.W. (deposition date: 2003-05-19, release date: 2004-01-20, Last modification date: 2024-05-22)

Primary citation

Van Ingen, H.,Lasonder, E.,Jansen, J.F.,Kaan, A.M.,Spronk, C.A.,Stunnenberg, H.G.,Vuister, G.W.
Extension of the binding motif of the sin3 interacting domain of the mad family proteins(,).
Biochemistry, 43:46-54, 2004

PubMed Abstract: Sin3 forms the scaffold for a multiprotein corepressor complex that silences transcription via the action of histone deacetylases. Sin3 is recruited to the DNA by several DNA binding repressors, such as the helix-loop-helix proteins of the Mad family. Here, we elaborate on the Mad-Sin3 interaction based on a binding study, solution structure, and dynamics of the PAH2 domain of mSin3 in complex to an extended Sin3 interacting domain (SID) of 24 residues of Mad1. We show that SID residues Met7 and Glu23, outside the previously defined minimal binding motif, mediate additional hydrophobic and electrostatic interactions with PAH2. On the basis of these results we propose an extended consensus sequence describing the PAH2-SID interaction specifically for the Mad family, showing that residues outside the hydrophobic core of the SID interact with PAH2 and modulate binding affinity to appropriate levels.

PubMed: 14705930

Experimental method

SOLUTION NMR