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1UB1

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

Summary for 1UB1
Entry DOI10.2210/pdb1ub1/pdb
NMR InformationBMRB: 4467
Descriptorattachment region binding protein (1 entity in total)
Functional Keywordschicken methyl-cpg-binding protein 2 (cmecp2), mar-binding protein (arbp), nmr spectroscopy, protein-dna interaction, structural proteomics in europe, spine, structural genomics, transcription
Biological sourceGallus gallus (chicken)
Total number of polymer chains1
Total formula weight14816.74
Authors
Heitmann, B.,Maurer, T.,Weitzel, J.M.,Stratling, W.H.,Kalbitzer, H.R.,Brunner, E.,Structural Proteomics in Europe (SPINE) (deposition date: 2003-03-27, release date: 2003-08-05, Last modification date: 2023-12-27)
Primary citationHeitmann, B.,Maurer, T.,Weitzel, J.M.,Stratling, W.H.,Kalbitzer, H.R.,Brunner, E.
Solution structure of the matrix attachment region-binding domain of chicken MeCP2
EUR.J.BIOCHEM., 270:3263-3270, 2003
Cited by
PubMed Abstract: 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.
PubMed: 12869202
DOI: 10.1046/j.1432-1033.2003.03714.x
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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