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PDBsum entry 4x23

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Top Page protein dna_rna ligands Protein-protein interface(s) links
Structural protein/DNA PDB id
4x23
Contents
Protein chains
95 a.a.
79 a.a.
102 a.a.
90 a.a.
22 a.a.
21 a.a.
DNA/RNA
Ligands
ASN-ARG-ILE-ARG-
LEU
SER-ASN-ARG

References listed in PDB file
Key reference
Title A conserved mechanism for centromeric nucleosome recognition by centromere protein cenp-C.
Authors H.Kato, J.Jiang, B.R.Zhou, M.Rozendaal, H.Feng, R.Ghirlando, T.S.Xiao, A.F.Straight, Y.Bai.
Ref. Science, 2013, 340, 1110-1113. [DOI no: 10.1126/science.1235532]
PubMed id 23723239
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.
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