2o4a
From Proteopedia
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Crystal Structure of the N-terminal CUT Domain of SATB1 Bound to Matrix Attachment Region DNA
Overview
Special AT-rich sequence binding protein 1 (SATB1) regulates gene, expression essential in immune T-cell maturation and switching of fetal, globin species, by binding to matrix attachment regions (MARs) of DNA and, inducing a local chromatin remodeling. Previously we have revealed a, five-helix structure of the N-terminal CUT domain, which is essentially, the folded region in the MAR-binding domain, of human SATB1 by NMR. Here, we determined crystal structure of the complex of the CUT domain and a MAR, DNA, in which the third helix of the CUT domain deeply enters the major, groove of DNA in the B-form. Bases of 5'-CTAATA-3' sequence are contacted, by this helix, through direct and water-mediated hydrogen bonds and apolar, and van der Waals contacts. Mutations at conserved base-contacting, residues, Gln402 and Gly403, reduced the DNA-binding activity, which, confirmed the importance of the observed interactions involving these, residues. A significant number of equivalent contacts are observed also, for typically four-helix POU-specific domains of POU-homologous proteins, indicating that these domains share a common framework of the DNA-binding, mode, recognizing partially similar DNA sequences.
About this Structure
2O4A is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for recognition of the matrix attachment region of DNA by transcription factor SATB1., Yamasaki K, Akiba T, Yamasaki T, Harata K, Nucleic Acids Res. 2007 Jul 25;. PMID:17652321
Page seeded by OCA on Wed Jan 23 14:12:31 2008
