4X23

CRYSTAL STRUCTURE OF CENP-C IN COMPLEX WITH THE NUCLEOSOME CORE PARTICLE

「4INM」から置き換えられました

4X23 の概要

• エントリーDOI: 10.2210/pdb4x23/pdb
• 関連するPDBエントリー: 4INM
• 分子名称: DNA (147-MER), Histone H3, Histone H4, ... (7 entities in total)
• 機能のキーワード: 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
• 由来する生物種: Homo sapiens; 詳細
• 細胞内の位置: Nucleus : P02299 P84040 P84051 P02283
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 359944.46

構造登録者

Jiang, J.S. (登録日: 2014-11-25, 公開日: 2014-12-10, 最終更新日: 2023-09-27)

主引用文献

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

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: 23723239
DOI: 10.1126/science.1235532

実験手法

X-RAY DIFFRACTION (3.5 Å)