2iij
Structure of human Asf1a in complex with histone H3
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OverviewOverview
Asf1 is a histone chaperone that favors histone H3/H4 assembly and, disassembly. We solved the structure of the conserved domain of human, ASF1A in complex with the C-terminal helix of histone H3 using nuclear, magnetic resonance spectroscopy. This structure is fully compatible with, an association of ASF1 with the heterodimeric form of histones H3/H4. In, our model, ASF1 substitutes for the second H3/H4 heterodimer that is, normally found in heterotetrameric H3/H4 complexes. This result, constitutes an essential step in the fundamental understanding of the, mechanisms of nucleosome assembly by histone chaperones. Point mutations, that perturb the Asf1/histone interface were designed from the structure., The decreased binding affinity of the Asf1-H3/H4 complex correlates with, decreased levels of H3-K56 acetylation and phenotypic defects in vivo.
About this StructureAbout this Structure
2IIJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the histone chaperone asf1 bound to the histone h3 C-terminal helix and functional insights., Agez M, Chen J, Guerois R, van Heijenoort C, Thuret JY, Mann C, Ochsenbein F, Structure. 2007 Feb;15(2):191-9. PMID:17292837
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