PTEN: Difference between revisions
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<StructureSection load='1d5r' size='350' side='right' caption='Human PTEN complex with tartaric acid (PDB entry [[1d5r]])' scene=''> | |||
==MUTATIONS OF PTEN IN CANCER== | ==MUTATIONS OF PTEN IN CANCER== | ||
'''PTEN''' is a tumor suppressor protein that is mutated in several human cancers. These include glioblastomas, endometrial carcinomas, prostate carcinomas, and melanoma cases. This protein is a phosphatase that acts on both polypeptide and phosphoinositide substrates [[http://images.google.com/imgres?imgurl=http://www.nature.com/nrc/journal/v7/n1/images/nrc2037-f1.jpg&imgrefurl=http://www.nature.com/nrc/journal/v7/n1/fig_tab/nrc2037_F1.html&usg=__3dbY0r1Jy39GDzgNvA1BJ-PxgmU=&h=362&w=505&sz=23&hl=en&start=5&um=1&tbnid=3OEbN1FJyVtexM:&tbnh=93&tbnw=130&prev=/images%3Fq%3DPTEN%26hl%3Den%26rls%3DGGLJ,GGLJ:2006-34,GGLJ:en%26sa%3DN%26um%3D1|(1)]]. PTEN has 403 amino acids which are separated into <scene name='Nathan_Line_sandbox/Structure/6'>two domains.</scene> The red section represents the C2 domain which allows the protein to bind with phospholipid membrane. The phosphatase section (blue) interacts with the ligand and the phosphate head. These interactions are controled by two separate loops. The <scene name='Nathan_Line_sandbox/Actice_site/1'>P-loop</scene> is responsible for the catalytic reactions performed by the protein. These reactions are what halt cell growth. The P-loop is made up of two parts, the catalytic parts (green) that perform the reactions and the conformational parts (purple) that force the loop into its conformational shape. The other loop is the <scene name='Nathan_Line_sandbox/Structure/5'>"TI" loop.</scene> This loop interacts with the lipid while in the active P-loop to increase the catalysis. | |||
PTEN is a tumor suppressor protein that is mutated in several human cancers. These include glioblastomas, endometrial carcinomas, prostate carcinomas, and melanoma cases. This protein is a phosphatase that acts on both polypeptide and phosphoinositide substrates [[http://images.google.com/imgres?imgurl=http://www.nature.com/nrc/journal/v7/n1/images/nrc2037-f1.jpg&imgrefurl=http://www.nature.com/nrc/journal/v7/n1/fig_tab/nrc2037_F1.html&usg=__3dbY0r1Jy39GDzgNvA1BJ-PxgmU=&h=362&w=505&sz=23&hl=en&start=5&um=1&tbnid=3OEbN1FJyVtexM:&tbnh=93&tbnw=130&prev=/images%3Fq%3DPTEN%26hl%3Den%26rls%3DGGLJ,GGLJ:2006-34,GGLJ:en%26sa%3DN%26um%3D1|(1)]]. PTEN has 403 amino acids which are separated into <scene name='Nathan_Line_sandbox/Structure/6'>two domains.</scene> The red section represents the C2 domain which allows the protein to bind with phospholipid membrane. The phosphatase section (blue) interacts with the ligand and the phosphate head. These interactions are controled by two separate loops. The <scene name='Nathan_Line_sandbox/Actice_site/1'>P-loop</scene> is responsible for the catalytic reactions performed by the protein. These reactions are what halt cell growth. The P-loop is made up of two parts, the catalytic parts (green) that perform the reactions and the conformational parts (purple) that force the loop into its conformational shape. The other loop is the <scene name='Nathan_Line_sandbox/Structure/5'>"TI" loop.</scene> This loop interacts with the lipid while in the active P-loop to increase the catalysis. | |||
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==Additional Resources== | ==Additional Resources== | ||
For Additional Information, See: [[Cancer]] | For Additional Information, See: | ||
*[[Cancer]] | |||
*[[Phosphoinositide phosphatase]] | |||
*[[Proteins involved in cancer]] | |||
==REFERENCES== | ==REFERENCES== | ||
<ref group="xtra">PMID:10555148</ref><references group="xtra"/> | <ref group="xtra">PMID:10555148</ref><references group="xtra"/> |