1tey
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(New page: 200px<br /> <applet load="1tey" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tey" /> '''NMR structure of human histone chaperone, A...)
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Revision as of 17:17, 12 November 2007
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NMR structure of human histone chaperone, ASF1A
Overview
Asf1 is a conserved histone chaperone implicated in nucleosome assembly, transcriptional silencing, and the cellular response to DNA damage. We, solved the NMR solution structure of the N-terminal functional domain of, the human Asf1a isoform, and we identified by NMR chemical shift mapping a, surface of Asf1a that binds the C-terminal helix of histone H3. This, binding surface forms a highly conserved hydrophobic groove surrounded by, charged residues. Mutations within this binding site decreased the, affinity of Asf1a for the histone H3/H4 complex in vitro, and the same, mutations in the homologous yeast protein led to transcriptional silencing, defects, DNA damage sensitivity, and thermosensitive growth. We have thus, obtained direct experimental evidence of the mode of binding between a, histone and one of its chaperones and genetic data suggesting that this, interaction is important in both the DNA damage response and, transcriptional silencing.
About this Structure
1TEY is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for the interaction of Asf1 with histone H3 and its functional implications., Mousson F, Lautrette A, Thuret JY, Agez M, Courbeyrette R, Amigues B, Becker E, Neumann JM, Guerois R, Mann C, Ochsenbein F, Proc Natl Acad Sci U S A. 2005 Apr 26;102(17):5975-80. Epub 2005 Apr 19. PMID:15840725
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