3N5U

Crystal structure of an Rb C-terminal peptide bound to the catalytic subunit of PP1

3N5U の概要

• エントリーDOI: 10.2210/pdb3n5u/pdb
• 分子名称: Serine/threonine-protein phosphatase PP1-alpha catalytic subunit, Retinoblastoma-associated protein, MANGANESE (II) ION, ... (4 entities in total)
• 機能のキーワード: retinoblastoma, prb, rb, protein phosphatase-1, pp1, phosphatase, hydrolase, transcription regulation
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: P62136; Nucleus: P06400
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 70566.22

構造登録者

Hirschi, A.M.,Cecchini, M.,Steinhardt, R.C.,Dick, F.A.,Rubin, S.M. (登録日: 2010-05-25, 公開日: 2010-08-11, 最終更新日: 2024-02-21)

主引用文献

Hirschi, A.,Cecchini, M.,Steinhardt, R.C.,Schamber, M.R.,Dick, F.A.,Rubin, S.M.
An overlapping kinase and phosphatase docking site regulates activity of the retinoblastoma protein.
Nat.Struct.Mol.Biol., 17:1051-1057, 2010

PubMed Abstract: The phosphorylation state and corresponding activity of the retinoblastoma tumor suppressor protein (Rb) are modulated by a balance of kinase and phosphatase activities. Here we characterize the association of Rb with the catalytic subunit of protein phosphatase 1 (PP1c). A crystal structure identifies an enzyme docking site in the Rb C-terminal domain that is required for efficient PP1c activity toward Rb. The phosphatase docking site overlaps with the known docking site for cyclin-dependent kinase (Cdk), and PP1 competition with Cdk-cyclins for Rb binding is sufficient to retain Rb activity and block cell-cycle advancement. These results provide the first detailed molecular insights into Rb activation and establish a novel mechanism for Rb regulation in which kinase and phosphatase compete for substrate docking.

PubMed: 20694007
DOI: 10.1038/nsmb.1868

実験手法

X-RAY DIFFRACTION (3.2 Å)