PTEN: Difference between revisions

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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.
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.


<scene name='Nathan_Line_sandbox/P_mutations/1'>TextToBeDisplayed</scene>
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>


<scene name='Nathan_Line_sandbox/Ti_mutations/1'>TextToBeDisplayed</scene>
<scene name='Nathan_Line_sandbox/Ti_mutations/1'>TextToBeDisplayed</scene>

Revision as of 01:02, 6 October 2009

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PDB ID 1d5r

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1d5r, resolution 2.10Å ()
Ligands:
Activity: Protein-tyrosine-phosphatase, with EC number 3.1.3.48
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



MUTATIONS OF PTEN IN CANCERMUTATIONS 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. PTEN has 403 amino acids which are separated into 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 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 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

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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