2AFF

The solution structure of the Ki67FHA/hNIFK(226-269)3P complex

2AFF の概要

• エントリーDOI: 10.2210/pdb2aff/pdb
• 関連するPDBエントリー: 1R21
• NMR情報: BMRB: 6748
• 分子名称: Antigen KI-67, MKI67 FHA domain interacting nucleolar phosphoprotein (2 entities in total)
• 機能のキーワード: ki67; fha; nifk; nmr; phosphoprotein, cell cycle
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: P46013; Nucleus, nucleolus: Q9BYG3
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19024.21

構造登録者

Byeon, I.-J.L.,Li, H.,Song, H.,Gronenborn, A.M.,Tsai, M.D. (登録日: 2005-07-25, 公開日: 2005-10-25, 最終更新日: 2024-10-30)

主引用文献

Byeon, I.J.,Li, H.,Song, H.,Gronenborn, A.M.,Tsai, M.D.
Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67.
Nat.Struct.Mol.Biol., 12:987-993, 2005

PubMed Abstract: The forkhead-associated (FHA) domain of human Ki67 interacts with the human nucleolar protein hNIFK, recognizing a 44-residue fragment, hNIFK226-269, phosphorylated at Thr234. Here we show that high-affinity binding requires sequential phosphorylation by two kinases, CDK1 and GSK3, yielding pThr238, pThr234 and pSer230. We have determined the solution structure of Ki67FHA in complex with the triply phosphorylated peptide hNIFK226-269(3P), revealing not only local recognition of pThr234 but also the extension of the beta-sheet of the FHA domain by the addition of a beta-strand of hNIFK. The structure of an FHA domain in complex with a biologically relevant binding partner provides insights into ligand specificity and potentially links the cancer marker protein Ki67 to a signaling pathway associated with cell fate specification.

PubMed: 16244663
DOI: 10.1038/nsmb1008

実験手法

SOLUTION NMR