2IIJ
Structure of human Asf1a in complex with histone H3
Summary for 2IIJ
| Entry DOI | 10.2210/pdb2iij/pdb |
| Related | 1tey |
| NMR Information | BMRB: 6298 |
| Descriptor | ASF1A protein, Histone H3 (2 entities in total) |
| Functional Keywords | protein-protein complex, chaperone |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 19931.36 |
| Authors | Agez, M.,Guerois, R.,van Heijenoort, C.,Mann, C.,Ochsenbein, F. (deposition date: 2006-09-28, release date: 2007-02-13, Last modification date: 2024-05-29) |
| Primary citation | Agez, M.,Chen, J.,Guerois, R.,van Heijenoort, C.,Thuret, J.Y.,Mann, C.,Ochsenbein, F. Structure of the histone chaperone asf1 bound to the histone h3 C-terminal helix and functional insights. Structure, 15:191-199, 2007 Cited by PubMed Abstract: 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. PubMed: 17292837DOI: 10.1016/j.str.2007.01.002 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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