1LGP

Crystal structure of the FHA domain of the Chfr mitotic checkpoint protein complexed with tungstate

1LGP の概要

• エントリーDOI: 10.2210/pdb1lgp/pdb
• 関連するPDBエントリー: 1LGQ
• 分子名称: cell cycle checkpoint protein CHFR, TUNGSTATE(VI)ION (3 entities in total)
• 機能のキーワード: chfr, fha, tungstate, domain swapping, checkpoint, cell cycle
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus, PML body : Q96EP1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13450.92

構造登録者

Stavridi, E.S.,Huyen, Y.,Loreto, I.R.,Scolnick, D.M.,Halazonetis, T.D.,Pavletich, N.P.,Jeffrey, P.D. (登録日: 2002-04-16, 公開日: 2002-05-08, 最終更新日: 2024-05-22)

主引用文献

Stavridi, E.S.,Huyen, Y.,Loreto, I.R.,Scolnick, D.M.,Halazonetis, T.D.,Pavletich, N.P.,Jeffrey, P.D.
Crystal structure of the FHA domain of the Chfr mitotic checkpoint protein and its complex with tungstate.
Structure, 10:891-899, 2002

PubMed Abstract: The Chfr mitotic checkpoint protein is frequently inactivated in human cancer. We determined the three-dimensional structure of its FHA domain in its native form and in complex with tungstate, an analog of phosphate. The structures revealed a beta sandwich fold similar to the previously determined folds of the Rad53 N- and C-terminal FHA domains, except that the Rad53 domains were monomeric, whereas the Chfr FHA domain crystallized as a segment-swapped dimer. The ability of the Chfr FHA domain to recognize tungstate suggests that it shares the ability with other FHA domains to bind phosphoproteins. Nevertheless, differences in the sequence and structure of the Chfr and Rad53 FHA domains suggest that FHA domains can be divided into families with distinct binding properties.

PubMed: 12121644
DOI: 10.1016/S0969-2126(02)00776-1

実験手法

X-RAY DIFFRACTION (2 Å)