7V6P
Crystal structure of human sNASP TPR domain
Summary for 7V6P
| Entry DOI | 10.2210/pdb7v6p/pdb |
| Descriptor | Isoform 2 of Nuclear autoantigenic sperm protein, GLYCEROL, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | histone chaperone, chaperone |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 32677.77 |
| Authors | |
| Primary citation | Liu, C.P.,Jin, W.,Hu, J.,Wang, M.,Chen, J.,Li, G.,Xu, R.M. Distinct histone H3-H4 binding modes of sNASP reveal the basis for cooperation and competition of histone chaperones. Genes Dev., 35:1610-1624, 2021 Cited by PubMed Abstract: Chromosomal duplication requires de novo assembly of nucleosomes from newly synthesized histones, and the process involves a dynamic network of interactions between histones and histone chaperones. sNASP and ASF1 are two major histone H3-H4 chaperones found in distinct and common complexes, yet how sNASP binds H3-H4 in the presence and absence of ASF1 remains unclear. Here we show that, in the presence of ASF1, sNASP principally recognizes a partially unfolded Nα region of histone H3, and in the absence of ASF1, an additional sNASP binding site becomes available in the core domain of the H3-H4 complex. Our study also implicates a critical role of the C-terminal tail of H4 in the transfer of H3-H4 between sNASP and ASF1 and the coiled-coil domain of sNASP in nucleosome assembly. These findings provide mechanistic insights into coordinated histone binding and transfer by histone chaperones. PubMed: 34819355DOI: 10.1101/gad.349100.121 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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