5K6S

The structure of the PP2A B56 subunit BubR1 complex

5K6S の概要

• エントリーDOI: 10.2210/pdb5k6s/pdb
• 分子名称: Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform, BubR1 (3 entities in total)
• 機能のキーワード: phosphatase, regulator, slim, cell cycle, hydrolase
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 43931.65

構造登録者

Page, R.,Wang, X.,Bajaj, R.,Peti, W. (登録日: 2016-05-25, 公開日: 2016-12-07, 最終更新日: 2024-10-23)

主引用文献

Wang, X.,Bajaj, R.,Bollen, M.,Peti, W.,Page, R.
Expanding the PP2A Interactome by Defining a B56-Specific SLiM.
Structure, 24:2174-2181, 2016

PubMed Abstract: Specific interactions between proteins govern essential physiological processes including signaling. Many enzymes, especially the family of serine/threonine phosphatases (PSPs: PP1, PP2A, and PP2B/calcineurin/CN), recruit substrates and regulatory proteins by binding short linear motifs (SLiMs), short sequences found within intrinsically disordered regions that mediate specific protein-protein interactions. While tremendous progress had been made in identifying where and how SLiMs bind PSPs, especially PP1 and CN, essentially nothing is known about how SLiMs bind PP2A, a validated cancer drug target. Here we describe three structures of a PP2A-SLiM interaction (B56:pS-RepoMan, B56:pS-BubR1, and B56:pSpS-BubR1), show that this PP2A-specific SLiM is defined as LSPIxE, and then use these data to discover scores of likely PP2A regulators and substrates. Together, these data provide a powerful approach not only for dissecting PP2A interaction networks in cells but also for targeting PP2A diseases, such as cancer.

PubMed: 27998540
DOI: 10.1016/j.str.2016.09.010

実験手法

X-RAY DIFFRACTION (2.794 Å)