2fxk
From Proteopedia
(New page: 200px<br /> <applet load="2fxk" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fxk, resolution 2.54Å" /> '''Crystal structure o...) |
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| - | [[Image:2fxk.gif|left|200px]]<br /> | + | [[Image:2fxk.gif|left|200px]]<br /><applet load="2fxk" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2fxk" size=" | + | |
caption="2fxk, resolution 2.54Å" /> | caption="2fxk, resolution 2.54Å" /> | ||
'''Crystal structure of the macro-domain of human core histone variant macroH2A1.1 (form A)'''<br /> | '''Crystal structure of the macro-domain of human core histone variant macroH2A1.1 (form A)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Histone macroH2A is a hallmark of mammalian heterochromatin. Here we show | + | 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 Structure== | ==About this Structure== | ||
| - | 2FXK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure | + | 2FXK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry 1ZQ0. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FXK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Hothorn, M.]] | [[Category: Hothorn, M.]] | ||
[[Category: Kustatscher, G.]] | [[Category: Kustatscher, G.]] | ||
| - | [[Category: Ladurner, A | + | [[Category: Ladurner, A G.]] |
[[Category: Pugieux, C.]] | [[Category: Pugieux, C.]] | ||
[[Category: Scheffzek, K.]] | [[Category: Scheffzek, K.]] | ||
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[[Category: p-loop]] | [[Category: p-loop]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:26:06 2008'' |
Revision as of 15:26, 21 February 2008
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Crystal structure of the macro-domain of human core histone variant macroH2A1.1 (form A)
Overview
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 Structure
2FXK is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1ZQ0. Full crystallographic information is available from OCA.
Reference
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 Thu Feb 21 17:26:06 2008
Categories: Homo sapiens | Single protein | Hothorn, M. | Kustatscher, G. | Ladurner, A G. | Pugieux, C. | Scheffzek, K. | A1pp | Chromatin | Histone | Macro-domain | P-loop
