2f5k
From Proteopedia
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| - | [[Image:2f5k.gif|left|200px]] | + | [[Image:2f5k.gif|left|200px]] |
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| - | '''Crystal structure of the chromo domain of human MRG15''' | + | {{Structure |
| + | |PDB= 2f5k |SIZE=350|CAPTION= <scene name='initialview01'>2f5k</scene>, resolution 2.200Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Crystal structure of the chromo domain of human MRG15''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2F5K is a [ | + | 2F5K is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F5K OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of human MRG15 chromo domain and its binding to Lys36-methylated histone H3., Zhang P, Du J, Sun B, Dong X, Xu G, Zhou J, Huang Q, Liu Q, Hao Q, Ding J, Nucleic Acids Res. 2006;34(22):6621-8. Epub 2006 Nov 28. PMID:[http:// | + | Structure of human MRG15 chromo domain and its binding to Lys36-methylated histone H3., Zhang P, Du J, Sun B, Dong X, Xu G, Zhou J, Huang Q, Liu Q, Hao Q, Ding J, Nucleic Acids Res. 2006;34(22):6621-8. Epub 2006 Nov 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17135209 17135209] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: gene regulation]] | [[Category: gene regulation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:48:21 2008'' |
Revision as of 14:48, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the chromo domain of human MRG15
Overview
Human MRG15 is a transcription factor that plays a vital role in embryonic development, cell proliferation and cellular senescence. It comprises a putative chromo domain in the N-terminal part that has been shown to participate in chromatin remodeling and transcription regulation. We report here the crystal structure of human MRG15 chromo domain at 2.2 A resolution. The MRG15 chromo domain consists of a beta-barrel and a long alpha-helix and assumes a structure more similar to the Drosophila MOF chromo barrel domain than the typical HP1/Pc chromo domains. The beta-barrel core contains a hydrophobic pocket formed by three conserved aromatic residues Tyr26, Tyr46 and Trp49 as a potential binding site for a modified residue of histone tail. However, the binding groove for the histone tail seen in the HP1/Pc chromo domains is pre-occupied by an extra beta-strand. In vitro binding assay results indicate that the MRG15 chromo domain can bind to methylated Lys36, but not methylated Lys4, Lys9 and Lys27 of histone H3. These data together suggest that the MRG15 chromo domain may function as an adaptor module which can bind to a modified histone H3 in a mode different from that of the HP1/Pc chromo domains.
About this Structure
2F5K is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of human MRG15 chromo domain and its binding to Lys36-methylated histone H3., Zhang P, Du J, Sun B, Dong X, Xu G, Zhou J, Huang Q, Liu Q, Hao Q, Ding J, Nucleic Acids Res. 2006;34(22):6621-8. Epub 2006 Nov 28. PMID:17135209
Page seeded by OCA on Thu Mar 20 16:48:21 2008
