Sandbox ggc16

2PQ8 Structure Myst Histone Acetyltransferase2PQ8 Structure Myst Histone Acetyltransferase

Part of the Myst Family, this histone modifier adds and removes a variety of chemical moieties to histone residues. Such modifications on a single or on several neighboring nucleosomes combine to produce a specific effect on the local chromatin structure. You may include any references to papers as in: the use of JSmol in Proteopedia or to the article describing Jmol to the rescue. Function Highly conserved in eukaryotes, their key roles in post-translation modification of histones. Profound effect on chromatin structure in eukaryotes. Composed of an Acetyl-CoA binding motif and a zinc finger. Disease residues of p53 acetylated by HATs may be located in variable sites, which leads to elevation of p53 DNA binding or loss of its transcriptional activity. It has been demonstrated that mutation of the C-terminal site of p53, where acetylation occurs, prompts comprehensively the loss of p53-dependent cyclin-dependent kinase inhibitor p21 transcription [49,50]. Acetylation of signal mediators may be prominent in subsequent stages in cancer progression.

spinqualitylabelsall models Myst Histone Acetyltransferase Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image