1ub1
From Proteopedia
(New page: 200px<br /><applet load="1ub1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ub1" /> '''Solution structure of the matrix attachment ...) |
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'''Solution structure of the matrix attachment region-binding domain of chicken MeCP2'''<br /> | '''Solution structure of the matrix attachment region-binding domain of chicken MeCP2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Methyl-CpG-binding protein 2 (MeCP2) is a multifunctional protein involved | + | 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== | ==About this Structure== | ||
| - | 1UB1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http:// | + | 1UB1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UB1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Brunner, E.]] | [[Category: Brunner, E.]] | ||
[[Category: Heitmann, B.]] | [[Category: Heitmann, B.]] | ||
| - | [[Category: Kalbitzer, H | + | [[Category: Kalbitzer, H R.]] |
[[Category: Maurer, T.]] | [[Category: Maurer, T.]] | ||
| - | [[Category: SPINE, Structural | + | [[Category: SPINE, Structural Proteomics in Europe.]] |
| - | [[Category: Stratling, W | + | [[Category: Stratling, W H.]] |
| - | [[Category: Weitzel, J | + | [[Category: Weitzel, J M.]] |
[[Category: chicken methyl-cpg-binding protein 2 (cmecp2)]] | [[Category: chicken methyl-cpg-binding protein 2 (cmecp2)]] | ||
[[Category: mar-binding protein (arbp)]] | [[Category: mar-binding protein (arbp)]] | ||
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[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:22:30 2008'' |
Revision as of 13:22, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 15:22:30 2008
Categories: Gallus gallus | Single protein | Brunner, E. | Heitmann, B. | Kalbitzer, H R. | Maurer, T. | SPINE, Structural Proteomics in Europe. | Stratling, W H. | Weitzel, J M. | Chicken methyl-cpg-binding protein 2 (cmecp2) | Mar-binding protein (arbp) | Nmr spectroscopy | Protein-dna interaction | Spine | Structural genomics | Structural proteomics in europe
