Crystal Structure of the PTEN Tumor
Suppressor
The structure of PTEN in cartoon view, the N-terminal in blue and the C-terminal in red.
- The PTEN gene codes for a 403 amino acid chain, and it contains signature motif of protein and tyrosine attached to each other, also it contains a phosphatase catalytic domain.
- The C-terminal tail consists of amino acids 353–403 and a loop present in the C2 region consists of amino acids 286–309. The C2 domain consists of amino acids 186–351 and the domain lacks the chelating residue Ca2+. The C2 and phosphatase domains form the minimal catalytic area of PTEN protein.
- The C-terminal has PDZ binding protein, which is important for stability and PTEN regulation.
- The PBD, which is located at the extreme N-terminus, is key in catalytic activity of PTEN and localization of membranes.
- The PTEN structure also contains an ‘N-terminal phosphatidylinositol-4, 5-bisphosphate-binding domain (PBD), which consists of amino acids 1-6.
this
figure shows the
2D structure of PTEN protein showing all the domains (Worby
& Dixon,
2014)
Lee,
J.O., Yang,
H., Georgescu,
M.M., Di
Cristofano, A., Maehama,
T., Shi,
Y., Dixon,
J.E., Pandolfi,
P., Pavletich,
N.P.
Crystal structure of the PTEN tumor suppressor: implications for
its phosphoinositide phosphatase activity and membrane
association.
(PubMed)
PDB ID (PDB)