Summary for 4X23
| Entry DOI | 10.2210/pdb4x23/pdb |
| Related | 4INM |
| Descriptor | DNA (147-MER), Histone H3, Histone H4, ... (7 entities in total) |
| Functional Keywords | nucleosome core particle, widom 601 dna fragmment, histone fold, cenp-c complex, segregation, chromosome centromere, kinetochore assembly, constitutive centromere-associated network (ccan) proteins, structural protein-dna complex, structural protein/dna |
| Biological source | Homo sapiens More |
| Cellular location | Nucleus : P02299 P84040 P84051 P02283 |
| Total number of polymer chains | 24 |
| Total formula weight | 359944.46 |
| Authors | Jiang, J.S. (deposition date: 2014-11-25, release date: 2014-12-10, Last modification date: 2023-09-27) |
| Primary citation | Kato, H.,Jiang, J.S.,Zhou, B.R.,Rozendaal, M.,Feng, H.,Ghirlando, R.,Xiao, T.S.,Straight, A.F.,Bai, Y. A conserved mechanism for centromeric nucleosome recognition by centromere protein CENP-C. Science, 340:1110-1113, 2013 Cited by PubMed Abstract: Chromosome segregation during mitosis requires assembly of the kinetochore complex at the centromere. Kinetochore assembly depends on specific recognition of the histone variant CENP-A in the centromeric nucleosome by centromere protein C (CENP-C). We have defined the determinants of this recognition mechanism and discovered that CENP-C binds a hydrophobic region in the CENP-A tail and docks onto the acidic patch of histone H2A and H2B. We further found that the more broadly conserved CENP-C motif uses the same mechanism for CENP-A nucleosome recognition. Our findings reveal a conserved mechanism for protein recruitment to centromeres and a histone recognition mode whereby a disordered peptide binds the histone tail through hydrophobic interactions facilitated by nucleosome docking. PubMed: 23723239DOI: 10.1126/science.1235532 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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