Heinrich, F.
, Chakravarthy, S.
, , H.
, Papa, A.
, , P.
, , A.
, , R.
, Gericke, A.
and Loesche, P.
(2015),
The PTEN Tumor Suppressor Forms Homodimers in Solution, Structure, [online], https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=918421
(Accessed April 28, 2024)
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The PTEN Tumor Suppressor Forms Homodimers in Solution
Published
Author(s)
, Srinivas Chakravarthy, , Antonella Papa, Pier Paolo Pandolfi, Alonzo H. Ross, Rakesh K. Harishchandra, Arne Gericke,
Abstract
The PTEN tumor suppressor exerts phosphatase activity on PI(3,4,5)P3 in the plasma membrane and was recently reported to dimerize in cell models. Here we show that PTEN forms homodimers in vitro and determine a structural model of the complex from SAXS and Rosetta docking studies. PTEN's C-terminal tail is disordered on the monomer but presumable well-folded on the dimer, shedding new light on its regulatory role.Citation
Structure
Volume
23
Pub Type
Journals
Download Paper
Keywords
PI3K/Akt pathway, PTEN phosphatase, dimer structure, SAXS, protein docking
Citation
Created August 21, 2015, Updated February 19, 2017