3X1S
Crystal structure of the nucleosome core particle
Summary for 3X1S
| Entry DOI | 10.2210/pdb3x1s/pdb |
| Related | 3X1T 3X1U 3X1V |
| Descriptor | Histone H3.1, Histone H4, Histone H2A type 1-B/E, ... (8 entities in total) |
| Functional Keywords | histones, nuclosome core particle, structural protein-dna complex, structural protein/dna |
| Biological source | Homo sapiens (human) More |
| Cellular location | Nucleus: P68431 P62805 P04908 P33778 |
| Total number of polymer chains | 10 |
| Total formula weight | 199415.50 |
| Authors | Sivaraman, P.,Kumarevel, T.S. (deposition date: 2014-11-27, release date: 2015-09-23, Last modification date: 2023-11-08) |
| Primary citation | Padavattan, S.,Shinagawa, T.,Hasegawa, K.,Kumasaka, T.,Ishii, S.,Kumarevel, T. Structural and functional analyses of nucleosome complexes with mouse histone variants TH2a and TH2b, involved in reprogramming Biochem.Biophys.Res.Commun., 464:929-935, 2015 Cited by PubMed Abstract: Histone variants TH2a and TH2b are highly expressed in testes, oocytes and zygotes. Our recent analysis suggested that these histone variants enhance the induced generation of pluripotent stem cells (iPSCs) when co-expressed along with four transcription factors, Oct3/4, Sox2, Klf4 and c-Myc (OSKM), and are associated with an open chromatin structure [1]. In the present study, we report the crystal structures of nucleosomes (NCPs) with the mouse histone variants, TH2a and TH2b. The structures revealed two significant changes, as compared to the canonical counterparts: fewer histone-DNA contacts and changes in dimer-dimer interactions between TH2a-TH2a' (L1-loop). In vivo studies with domain swapping and point mutants of the variants revealed that the residues in the histone tails and the TH2a-L1 loop are important for reprogramming. Taken together, our work indicates that the NCP variants with structural modifications and flexible tails are most likely important for enhanced reprogramming of functions. PubMed: 26188507DOI: 10.1016/j.bbrc.2015.07.070 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.805 Å) |
Structure validation
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