5DV2

Crystal structure of human CNOT6L in complex with cytidine-5'-monophosphate

5DV2 の概要

• エントリーDOI: 10.2210/pdb5dv2/pdb
• 関連するPDBエントリー: 5DV4
• 分子名称: CCR4-NOT transcription complex subunit 6-like, CYTIDINE-5'-MONOPHOSPHATE (3 entities in total)
• 機能のキーワード: nuclease domain, deadenylase, inhibitor complex, hydrolase
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm: Q96LI5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 45463.70

構造登録者

Zhang, Q.,Bartlam, M. (登録日: 2015-09-21, 公開日: 2016-05-18, 最終更新日: 2024-03-20)

主引用文献

Zhang, Q.,Yan, D.,Guo, E.,Ding, B.,Yang, W.,Liu, R.,Yamamoto, T.,Bartlam, M.
Structural basis for inhibition of the deadenylase activity of human CNOT6L
Febs Lett., 590:1270-1279, 2016

PubMed Abstract: Human CNOT6L/CCR4, a member of the endonuclease-exonuclease-phosphatase (EEP) family enzymes, is one of the two deadenylase enzymes in the conserved CCR4-NOT complex. Here, we report inhibitor-bound crystal structures of the human CNOT6L nuclease domain in complex with the nucleotide CMP and the aminoglycoside neomycin. Deadenylase activity assays show that nucleotides are effective inhibitors of both CNOT6L and CNOT7, with AMP more effective than other nucleotides, and that neomycin is a weak deadenylase inhibitor. Structural analysis shows that all inhibitors occupy the substrate and magnesium-binding sites of CNOT6L, suggesting that inhibitors compete with both substrate and divalent magnesium ions for overlapping binding sites.

PubMed: 27013054
DOI: 10.1002/1873-3468.12160

実験手法

X-RAY DIFFRACTION (2.07 Å)