1zr5
Crystal structure of the macro-domain of human core histone variant macroH2A1.2
OverviewOverview
Histone macroH2A is a hallmark of mammalian heterochromatin. Here we show that human macroH2A1.1 binds the SirT1-metabolite O-acetyl-ADP-ribose (OAADPR) through its macro domain. The 1.6-A crystal structure and mutants reveal how the metabolite is recognized. Mutually exclusive exon use in the gene H2AFY produces macroH2A1.2, whose tissue distribution differs. MacroH2A1.2 shows only subtle structural changes but cannot bind nucleotides. Alternative splicing may thus regulate the binding of nicotinamide adenine dinucleotide (NAD) metabolites to chromatin.
About this StructureAbout this Structure
1ZR5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Splicing regulates NAD metabolite binding to histone macroH2A., Kustatscher G, Hothorn M, Pugieux C, Scheffzek K, Ladurner AG, Nat Struct Mol Biol. 2005 Jul;12(7):624-5. Epub 2005 Jun 19. PMID:15965484 Page seeded by OCA on Sat May 3 17:57:57 2008