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Crystal structure of human phosphatase PTEN in its reduced state




Secondary structure is represented in cartoon visualization that is in color group.
Substrate dephosphorylation by PTEN, is dependent on the C residue in Red that acts as the thiol anion, this means that oxidation reactions can cause deactivation of the catalytic activity. The oxidation mechanism of inactivation, mostly occurs in the cell. The ‘Reactive oxygen species (ROS),’ which are usually in form of hydrogen peroxide are produced in the cell.
 

In this one is showing chain A is colored blue and chain B is colored green. The sulfurs of the cysteines are colored yellow. Two disulfides form between the two chains. A third disulfide is within Chain A.

The peroxides react with PTEN, resulting in the formation of a disulphide bonding in the catalytic area. The bond is usually formed between the amino acid residues C71 and C124. A compound called peroxiredoxin I, usually protects the PTEN protein from oxidation by peroxide.

 

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Redox Modulation of PTEN Phosphatase Activity by Hydrogen Peroxide and Bisperoxidovanadium Complexes.
Lee, C.U.Hahne, G.Hanske, J.Bange, T.Bier, D.Rademacher, C.Hennig, S.Grossmann, T.N.

 (PubMed)

 (PDB)