1UFI

Crystal structure of the dimerization domain of human CENP-B

1UFI の概要

• エントリーDOI: 10.2210/pdb1ufi/pdb
• 分子名称: Major centromere autoantigen B (2 entities in total)
• 機能のキーワード: dimerization domain, salt bridge, riken structural genomics/proteomics initiative, rsgi, structural genomics, dna binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: P07199
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 28997.14

構造登録者

Tawaramoto, M.S.,Kurumizaka, H.,Tanaka, Y.,Park, S.-Y.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2003-05-30, 公開日: 2004-02-17, 最終更新日: 2023-12-27)

主引用文献

Tawaramoto, M.S.,Park, S.-Y.,Tanaka, Y.,Nureki, O.,Kurumizaka, H.,Yokoyama, S.
Crystal structure of the human centromere protein B (CENP-B) dimerization domain at 1.65-A resolution
J.Biol.Chem., 278:51454-51461, 2003

PubMed Abstract: The human centromere protein B (CENP-B), a centromeric heterochromatin component, forms a homodimer that specifically binds to a distinct DNA sequence (the CENP-B box), which appears within every other alpha-satellite repeat. Previously, we determined the structure of the human CENP-B DNA-binding domain, CENP-B-(1-129), complexed with the CENP-B box DNA. In the present study, we determined the crystal structure of its dimerization domain (CENP-B-(540-599)), another functional domain of CENP-B, at 1.65-A resolution. CENP-B-(540-599) contains two alpha-helices, which are folded into an antiparallel configuration. The CENP-B-(540-599) dimer formed a symmetrical, antiparallel, four-helix bundle structure with a large hydrophobic patch in which 23 residues of one monomer form van der Waals contacts with the other monomer. In the CENP-B-(540-599) dimer, the N-terminal ends of CENP-B-(540-599) are oriented on opposite sides of the dimer. This CENP-B dimer configuration may be suitable for capturing two distant CENP-B boxes during centromeric heterochromatin formation.

PubMed: 14522975
DOI: 10.1074/jbc.M310388200

実験手法

X-RAY DIFFRACTION (1.65 Å)