1yse
From Proteopedia
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Solution structure of the MAR-binding domain of SATB1
Overview
SATB1 is a transcriptional regulator controlling the gene expression that, is essential in the maturation of the immune T-cell. SATB1 binds to the, nuclear matrix attachment regions of DNA, where it recruits histone, deacetylase and represses transcription through a local chromatin, remodeling. Here we determined the solution structure of the matrix, attachment region-binding domain, possessing similarity to the CUT, DNA-binding domain, of human SATB1 by NMR spectroscopy. The structure, consists of five alpha-helices, in which the N-terminal four are arranged, similarly to the four-helix structure of the CUT domain of hepatocyte, nuclear factor 6alpha. By an NMR chemical shift perturbation analysis and, by surface plasmon resonance analyses of SATB1 mutant proteins, an, interface for DNA binding was revealed to be located at the third helix, and the surrounding regions. Surface plasmon resonance experiments using, groove-specific binding drugs and methylated DNAs indicated that the, domain recognizes DNA from the major groove side. These observations, suggested that SATB1 possesses a DNA-binding mode similar to that of the, POU-specific DNA-binding domain, which is known to share structural, similarity to the four-helix CUT domain.
About this Structure
1YSE is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure and DNA-binding mode of the matrix attachment region-binding domain of the transcription factor SATB1 that regulates the T-cell maturation., Yamaguchi H, Tateno M, Yamasaki K, J Biol Chem. 2006 Feb 24;281(8):5319-27. Epub 2005 Dec 21. PMID:16371359
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