1ub1

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Solution structure of the matrix attachment region-binding domain of chicken MeCP2

Overview

Methyl-CpG-binding protein 2 (MeCP2) is a multifunctional protein involved, in chromatin organization and silencing of methylated DNA. MAR-BD, a, 125-amino-acid residue domain of chicken MeCP2 (cMeCP2, originally named, ARBP), is the minimal protein fragment required to recognize MAR elements, and mouse satellite DNA. Here we report the solution structure of MAR-BD, as determined by multidimensional heteronuclear NMR spectroscopy. The, global fold of this domain is very similar to that of rat MeCP2 MBD and, MBD1 MBD (the methyl-CpG-binding domains of rat MeCP2 and, methyl-CpG-binding domain protein 1, respectively), exhibiting a, three-stranded antiparallel beta-sheet and an alpha-helix alpha1. We show, that the C-terminal portion of MAR-BD also contains an amphipathic helical, coil, alpha2/alpha3. The hydrophilic residues of this coil form a surface, opposite the DNA interface, available for interactions with other domains, of MeCP2 or other proteins. Spectroscopic studies of the complex formed by, MAR-BD and a 15-bp fragment of a high-affinity binding site from mouse, satellite DNA indicates that the coil is also involved in protein.DNA, interactions. These studies provide a basis for discussion of the, consequences of six missense mutations within the helical coil found in, Rett syndrome cases.

About this Structure

1UB1 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

Solution structure of the matrix attachment region-binding domain of chicken MeCP2., Heitmann B, Maurer T, Weitzel JM, Stratling WH, Kalbitzer HR, Brunner E, Eur J Biochem. 2003 Aug;270(15):3263-70. PMID:12869202

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