PMID- 10555148
OWN - NLM
STAT- MEDLINE
DCOM- 19991123
LR  - 20190705
IS  - 0092-8674 (Print)
IS  - 0092-8674 (Linking)
VI  - 99
IP  - 3
DP  - 1999 Oct 29
TI  - Crystal structure of the PTEN tumor suppressor: implications for its
      phosphoinositide phosphatase activity and membrane association.
PG  - 323-34
AB  - The PTEN tumor suppressor is mutated in diverse human cancers and in hereditary
      cancer predisposition syndromes. PTEN is a phosphatase that can act on both
      polypeptide and phosphoinositide substrates in vitro. The PTEN structure reveals 
      a phosphatase domain that is similar to protein phosphatases but has an enlarged 
      active site important for the accommodation of the phosphoinositide substrate.
      The structure also reveals that PTEN has a C2 domain. The PTEN C2 domain binds
      phospholipid membranes in vitro, and mutation of basic residues that could
      mediate this reduces PTEN's membrane affinity and its ability to suppress the
      growth of glioblastoma tumor cells. The phosphatase and C2 domains associate
      across an extensive interface, suggesting that the C2 domain may serve to
      productively position the catalytic domain on the membrane.
FAU - Lee, J O
AU  - Lee JO
AD  - Cellular Biochemistry and Biophysics Program, Howard Hughes Medical Institute,
      Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.
FAU - Yang, H
AU  - Yang H
FAU - Georgescu, M M
AU  - Georgescu MM
FAU - Di Cristofano, A
AU  - Di Cristofano A
FAU - Maehama, T
AU  - Maehama T
FAU - Shi, Y
AU  - Shi Y
FAU - Dixon, J E
AU  - Dixon JE
FAU - Pandolfi, P
AU  - Pandolfi P
FAU - Pavletich, N P
AU  - Pavletich NP
LA  - eng
SI  - GENBANK/AF144732
SI  - PDB/1D5R
GR  - CA09673/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cell
JT  - Cell
JID - 0413066
RN  - 0 (Phosphatidylinositols)
RN  - 0 (Tumor Suppressor Proteins)
RN  - EC 3.1.3.2 (Phosphoric Monoester Hydrolases)
RN  - EC 3.1.3.67 (PTEN Phosphohydrolase)
RN  - EC 3.1.3.67 (PTEN protein, human)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - Caenorhabditis elegans
MH  - Computer Graphics
MH  - Crystallography, X-Ray/methods
MH  - Drosophila
MH  - *Genes, Tumor Suppressor
MH  - Humans
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - PTEN Phosphohydrolase
MH  - Phosphatidylinositols/metabolism
MH  - Phosphoric Monoester Hydrolases/*chemistry/*metabolism
MH  - Protein Structure, Secondary
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - *Tumor Suppressor Proteins
MH  - Xenopus
EDAT- 1999/11/11 00:00
MHDA- 1999/11/11 00:01
CRDT- 1999/11/11 00:00
PHST- 1999/11/11 00:00 [pubmed]
PHST- 1999/11/11 00:01 [medline]
PHST- 1999/11/11 00:00 [entrez]
AID - S0092-8674(00)81663-3 [pii]
AID - 10.1016/s0092-8674(00)81663-3 [doi]
PST - ppublish
SO  - Cell. 1999 Oct 29;99(3):323-34. doi: 10.1016/s0092-8674(00)81663-3.