3x1s | pdb_00003x1s

Crystal structure of the nucleosome core particle

spinqualitylabelsall models 3x1s, resolution 2.81Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3x1s is a 10 chain structure with sequence from Homo sapiens and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.805Å Ligands: CL, MN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function H4_HUMAN Publication Abstract from PubMed 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. Structural and functional analyses of nucleosome complexes with mouse histone variants TH2a and TH2b, involved in reprogramming.,Padavattan S, Shinagawa T, Hasegawa K, Kumasaka T, Ishii S, Kumarevel T Biochem Biophys Res Commun. 2015 Aug 28;464(3):929-35. doi:, 10.1016/j.bbrc.2015.07.070. Epub 2015 Jul 17. PMID:26188507 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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