D
IPR017884

SANT domain

InterPro entry
Short nameSANT_dom
Overlapping
homologous
superfamilies
 
domain relationships

Description

The SANT domain is a motif of ~50 amino acids present in proteins involved in chromatin-remodelling and transcription regulation. This eukaryotic domain was identified in nuclear receptor co-repressors and named after switching-defective protein 3 (Swi3), adaptor 2 (Ada2), nuclear receptor co-repressor (N-CoR) and transcription factor (TF)IIIB
[1]
. Although SANT domains show remarkable sequence and structural similarity to the DNA-binding helix-turn-helix (HTH) domain of the myb-like tandem repeat, their function is not DNA binding. Instead, SANT domains are protein-protein interaction modules and some can bind to histone tails (e.g. in Ada2 and SMRT). The SANT domain has been proposed to function as a histone-interaction module that couples histone-tail binding to enzyme catalysis for the remodelling of nucleosomes
[2, 3]
.

SANT domains are found in combination with other domains, such as the SWIRM domain (
IPR007526
), the ZZ-type zinc finger (see
IPR000433
), the C2H2-type zinc finger, the GATA-type zinc finger (
IPR000679
), the MPN-domain and DEAH ATP-helicase domain.

References

1.The SANT domain: a putative DNA-binding domain in the SWI-SNF and ADA complexes, the transcriptional co-repressor N-CoR and TFIIIB. Aasland R, Stewart AF, Gibson T. Trends Biochem. Sci. 21, 87-8, (1996). View articlePMID: 8882580

2.Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI. Grune T, Brzeski J, Eberharter A, Clapier CR, Corona DF, Becker PB, Muller CW. Mol. Cell 12, 449-60, (2003). View articlePMID: 14536084

3.The SANT domain: a unique histone-tail-binding module? Boyer LA, Latek RR, Peterson CL. Nat. Rev. Mol. Cell Biol. 5, 158-63, (2004). View articlePMID: 15040448

Cross References

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