|PROSITE documentation PDOC51477 [for PROSITE entry PS51477]|
The paired amphipathic helix (PAH) domain is a protein-protein interaction domain present in eukaryotic proteins implied in transcription down-regulation, such as the SIN3 family of proteins. This domain occurs generally in repeats at the N-terminus of the protein containing it . Sin3a is the central component of a transcriptional co-repressor complex that comprises the histone deacetylase (HDAC) 1 and 2. The three PAH domains of Sin3a associate with numerous DNA-binding proteins enabling the recruitment of the Sin3 complex to chromatin. PAH1 is known to interact so far with Opi1, Pf1, NRSF, N-CoR and SMRT while PAH2 interacts with a broader range of proteins including Mad protein family members, Sp1-like repressor proteins, HBP1, Pf1 and yeast Ume6 [2,3].
The 3D structure of the PAH domain has been determined. The PAH domain folds into a left-handed, four-helix bundle structure (see <PDB:2RMS> and <PDB:1G1E>). The amino acids in each of the helices and in the turn regions are arranged in such a way as to form a hydrophic cleft that constitutes the main surface of interaction with the Sin3 interaction domain (SID) amphipathic helix of transcription inhibitors such as SAP25 or Mad1 [1,4].
The profile we developed covers the entire PAH domain.Last update:
February 2010 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Sahu S.C. Swanson K.A. Kang R.S. Huang K. Brubaker K. Ratcliff K. Radhakrishnan I.|
|Title||Conserved themes in target recognition by the PAH1 and PAH2 domains of the Sin3 transcriptional corepressor.|
|Source||J. Mol. Biol. 375:1444-1456(2008).|
|2||Authors||Le Guezennec X. Vermeulen M. Stunnenberg H.G.|
|Title||Molecular characterization of Sin3 PAH-domain interactor specificity and identification of PAH partners.|
|Source||Nucleic Acids Res. 34:3929-3937(2006).|
|3||Authors||Spronk C.A. Tessari M. Kaan A.M. Jansen J.F. Vermeulen M. Stunnenberg H.G. Vuister G.W.|
|Title||The Mad1-Sin3B interaction involves a novel helical fold.|
|Source||Nat. Struct. Biol. 7:1100-1104(2000).|
|4||Authors||Brubaker K. Cowley S.M. Huang K. Loo L. Yochum G.S. Ayer D.E. Eisenman R.N. Radhakrishnan I.|
|Title||Solution structure of the interacting domains of the Mad-Sin3 complex: implications for recruitment of a chromatin-modifying complex.|