Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6L9H

The Human Telomeric Nucleosome Displays Distinct Structural and Dynamic Properties

Summary for 6L9H
Entry DOI10.2210/pdb6l9h/pdb
DescriptorHistone H3.1, Histone H4, Histone H2A type 1-B/E, ... (8 entities in total)
Functional Keywordstelomeric dna, nucleosome core particle, dna binding protein, dna binding protein-dna complex, dna binding protein/dna
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains10
Total formula weight176474.08
Authors
Soman, A.,Liew, C.W.,Teo, H.L.,Berezhnoy, N.,Korolev, N.,Rhodes, D.,Nordenskiold, L. (deposition date: 2019-11-10, release date: 2020-04-22, Last modification date: 2023-11-22)
Primary citationSoman, A.,Liew, C.W.,Teo, H.L.,Berezhnoy, N.V.,Olieric, V.,Korolev, N.,Rhodes, D.,Nordenskiold, L.
The human telomeric nucleosome displays distinct structural and dynamic properties.
Nucleic Acids Res., 48:5383-5396, 2020
Cited by
PubMed Abstract: Telomeres protect the ends of our chromosomes and are key to maintaining genomic integrity during cell division and differentiation. However, our knowledge of telomeric chromatin and nucleosome structure at the molecular level is limited. Here, we aimed to define the structure, dynamics as well as properties in solution of the human telomeric nucleosome. We first determined the 2.2 Å crystal structure of a human telomeric nucleosome core particle (NCP) containing 145 bp DNA, which revealed the same helical path for the DNA as well as symmetric stretching in both halves of the NCP as that of the 145 bp '601' NCP. In solution, the telomeric nucleosome exhibited a less stable and a markedly more dynamic structure compared to NCPs containing DNA positioning sequences. These observations provide molecular insights into how telomeric DNA forms nucleosomes and chromatin and advance our understanding of the unique biological role of telomeres.
PubMed: 32374876
DOI: 10.1093/nar/gkaa289
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon