2F5K

Crystal structure of the chromo domain of human MRG15

Summary for 2F5K

• Entry DOI: 10.2210/pdb2f5k/pdb
• Related: 2F5J 2F5L
• Descriptor: Mortality factor 4-like protein 1 (2 entities in total)
• Functional Keywords: beta barrel, gene regulation
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 6
• Total formula weight: 73506.86

Authors

Zhang, P.,Du, J.,Ding, J. (deposition date: 2005-11-26, release date: 2006-11-14, Last modification date: 2024-03-13)

Primary citation

Zhang, P.,Du, J.,Sun, B.,Dong, X.,Xu, G.,Zhou, J.,Huang, Q.,Liu, Q.,Hao, Q.,Ding, J.
Structure of human MRG15 chromo domain and its binding to Lys36-methylated histone H3.
Nucleic Acids Res., 34:6621-6628, 2006

PubMed Abstract: 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.

PubMed: 17135209
DOI: 10.1093/nar/gkl989

Experimental method

X-RAY DIFFRACTION (2.2 Å)