5SWF

The structure of the PP2A B56 subunit double phosphorylated BubR1 complex

Summary for 5SWF

• Entry DOI: 10.2210/pdb5swf/pdb
• Related: 5SW9
• Descriptor: Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform, Double phosphorylated BubR1 (3 entities in total)
• Functional Keywords: phosphatase, regulator, slim, cell cycle, hydrolase
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 42829.32

Authors

Page, R.,Wang, X.,Bajaj, R.,Peti, W. (deposition date: 2016-08-08, release date: 2016-11-30, Last modification date: 2023-10-04)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.818 Å)