{PDOC51477}
{PS51477; PAH}
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* PAH domain profile *
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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 [1]. 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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: February 2010 / First entry.

[1]  Sahu S.C., Swanson K.A., Kang R.S., Huang K., Brubaker K.,
     Ratcliff K., Radhakrishnan I.
     "Conserved themes in target recognition by the PAH1 and PAH2 domains
     of the Sin3 transcriptional corepressor."
     J. Mol. Biol. 375:1444-1456(2008).
     PubMed=18089292; DOI=10.1016/j.jmb.2007.11.079
[2]  Le Guezennec X., Vermeulen M., Stunnenberg H.G.
     "Molecular characterization of Sin3 PAH-domain interactor specificity
     and identification of PAH partners."
     Nucleic Acids Res. 34:3929-3937(2006).
     PubMed=16914451; DOI=10.1093/nar/gkl53
[3]  Spronk C.A., Tessari M., Kaan A.M., Jansen J.F., 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=11101889; DOI=10.1038/81944
[4]  Brubaker K., Cowley S.M., Huang K., Loo L., Yochum G.S., Ayer D.E.,
     Eisenman R.N., Radhakrishnan I.
     "Solution structure of the interacting domains of the Mad-Sin3
     complex: implications for recruitment of a chromatin-modifying
     complex."
     Cell 103:655-665(2000).
     PubMed=11106735

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