PTEN: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Nathan Line, Ann Taylor, David Canner, Michal Harel, Alexander Berchansky

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 PTEN is a tumor suppressor protein that is mutated in several human cancers.  These include glioblastomas, endometrial carcinomas, prostate carcinomas, and melanoma cases.  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.
-Mutations of PTEN occur within of the these different areas of the protein.  The P-loop itself contains three mutations all of which decrease the protein's activity. This results in excessive cells growth and tumors.  The amino acid mutated in the loop are <scene name='Nathan_Line_sandbox/P_mutations/1'>Lys125, Lys128, and His123</scene>, which decrease the protein's activity from 50-60%.
+Mutations of PTEN occur within of the these different areas of the protein.  The P-loop itself contains three mutations all of which decrease the protein's activity. This results in excessive cells growth and tumors.  The amino acid mutated in the loop are <scene name='Nathan_Line_sandbox/P_mutations/1'>Lys125, Lys128, and His123</scene>, which decrease the protein's activity from 50-60%.  The "TI" loop also contain mutations.  These include mutations of <scene name='Nathan_Line_sandbox/Ti_mutations/1'>Thr167 and Gln171.</scene>  Though the Gln171 mutation is not directly inside the "TI" loop, its close proximity does affect the loop's function.  These mutations decrease the activity by 60% and 75%.  Even though this loop is not a part of the catalysis, its decreased interactions with the lipid hinders the catalytic reactions of the P-loop.
-<scene name='Nathan_Line_sandbox/Ti_mutations/1'>TextToBeDisplayed</scene>
 <scene name='Nathan_Line_sandbox/C2_mutations/1'>TextToBeDisplayed</scene>