1Q4K

The polo-box domain of Plk1 in complex with a phospho-peptide

1Q4K の概要

• エントリーDOI: 10.2210/pdb1q4k/pdb
• 分子名称: Serine/threonine-protein kinase PLK, Phospho-peptide sequence Met.Gln.Ser.pThr.Pro.Leu (3 entities in total)
• 機能のキーワード: six-stranded anti-parallel beta sheet with one alpha helix, transferase
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: P53350
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 91853.43

構造登録者

Cheng, K.,Lowe, E.D.,Sinclair, J.,Nigg, E.A.,Johnson, L.N. (登録日: 2003-08-04, 公開日: 2003-11-11, 最終更新日: 2024-11-20)

主引用文献

Cheng, K.Y.,Lowe, E.D.,Sinclair, J.,Nigg, E.A.,Johnson, L.N.
The crystal structure of the human polo-like kinase-1 polo box domain and its phospho-peptide complex.
Embo J., 22:5757-5768, 2003

PubMed Abstract: Human polo-like kinase Plk1 localizes to the centrosomes, kinetochores and central spindle structures during mitosis. It plays an essential role in promoting mitosis and cytokinesis through phosphorylation of a number of different substrates. Kinase activity is regulated by a conserved C-terminal domain, termed the polo box domain (PBD), which acts both as an autoinhibitory domain and as a subcellular localization domain. We have determined the crystal structure of Plk1 PBD (residues 367-603) to 2.2 A resolution and the structure of a phospho-peptide-PBD (residues 345-603) complex to 2.3 A resolution. The two polo boxes of the PBD exhibit identical folds based on a six-stranded beta-sheet and an alpha-helix, despite only 12% sequence identity. The phospho-peptide binds at a site between the two polo boxes. It makes a short antiparallel beta-sheet connection and critical contacts to residues Trp414, Leu490, His538 and Lys540. Most of these residues had been shown to be important for biological activity through mutational studies. The results provide an explanation for phospho-peptide recognition and create the basis for new functional studies.

PubMed: 14592974
DOI: 10.1093/emboj/cdg558

実験手法

X-RAY DIFFRACTION (2.3 Å)