2pkg
From Proteopedia
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Structure of a complex between the A subunit of protein phosphatase 2A and the small t antigen of SV40
Overview
The small t antigen (ST) of DNA tumor virus SV40 facilitates cellular, transformation by disrupting the functions of protein phosphatase 2A, (PP2A) through a poorly defined mechanism. The crystal structure of the, core domain of SV40 ST bound to the scaffolding subunit of human PP2A, reveals that the ST core domain has a novel zinc-binding fold and, interacts with the conserved ridge of HEAT repeats 3-6, which overlaps, with the binding site for the B' (also called PR61 or B56) regulatory, subunit. ST has a lower binding affinity than B' for the PP2A core enzyme., Consequently, ST does not efficiently displace B' from PP2A holoenzymes in, vitro. Notably, ST inhibits PP2A phosphatase activity through its, N-terminal J domain. These findings suggest that ST may function mainly by, inhibiting the phosphatase activity of the PP2A core enzyme, and to a, lesser extent by modulating assembly of the PP2A holoenzymes.
About this Structure
2PKG is a Protein complex structure of sequences from Homo sapiens and Simian virus 40 with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Structural and biochemical insights into the regulation of protein phosphatase 2A by small t antigen of SV40., Chen Y, Xu Y, Bao Q, Xing Y, Li Z, Lin Z, Stock JB, Jeffrey PD, Shi Y, Nat Struct Mol Biol. 2007 Jun;14(6):527-34. Epub 2007 May 27. PMID:17529992
Page seeded by OCA on Mon Nov 12 23:24:38 2007
