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| | ==Solution structure of the matrix attachment region-binding domain of chicken MeCP2== | | ==Solution structure of the matrix attachment region-binding domain of chicken MeCP2== |
| - | <StructureSection load='1ub1' size='340' side='right'caption='[[1ub1]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='1ub1' size='340' side='right'caption='[[1ub1]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ub1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UB1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UB1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ub1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UB1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UB1 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ub1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ub1 OCA], [http://pdbe.org/1ub1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ub1 RCSB], [http://www.ebi.ac.uk/pdbsum/1ub1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ub1 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ub1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ub1 OCA], [https://pdbe.org/1ub1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ub1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ub1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ub1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O42403_CHICK O42403_CHICK] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chick]] | + | [[Category: Gallus gallus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Brunner, E]] | + | [[Category: Brunner E]] |
| - | [[Category: Heitmann, B]] | + | [[Category: Heitmann B]] |
| - | [[Category: Kalbitzer, H R]] | + | [[Category: Kalbitzer HR]] |
| - | [[Category: Maurer, T]] | + | [[Category: Maurer T]] |
| - | [[Category: SPINE, Structural Proteomics in Europe]]
| + | [[Category: Stratling WH]] |
| - | [[Category: Stratling, W H]] | + | [[Category: Weitzel JM]] |
| - | [[Category: Weitzel, J M]] | + | |
| - | [[Category: Nmr spectroscopy]]
| + | |
| - | [[Category: Protein-dna interaction]]
| + | |
| - | [[Category: Spine]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Structural proteomics in europe]]
| + | |
| - | [[Category: Transcription]]
| + | |
| Structural highlights
Function
O42403_CHICK
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Heitmann B, Maurer T, Weitzel JM, Stratling WH, Kalbitzer HR, Brunner E. Solution structure of the matrix attachment region-binding domain of chicken MeCP2. Eur J Biochem. 2003 Aug;270(15):3263-70. PMID:12869202
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