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1zr5

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1zr5, resolution 2.92Å ()
Domains: Macro_H2A_like
Related: 1zq0, 1zr3
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the macro-domain of human core histone variant macroH2A1.2

Publication Abstract from PubMed

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.

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1ZR5 is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Kustatscher G, Hothorn M, Pugieux C, Scheffzek K, Ladurner AG. Splicing regulates NAD metabolite binding to histone macroH2A. Nat Struct Mol Biol. 2005 Jul;12(7):624-5. Epub 2005 Jun 19. PMID:15965484 doi:10.1038/nsmb956

Page seeded by OCA on Tue Feb 17 12:14:02 2009

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