PTEN: Difference between revisions

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===MUTATIONS OF PTEN IN CANCER===
===MUTATIONS OF PTEN IN CANCER===


PTEN is often mutated in cancerIt has <scene name='Nathan_Line_sandbox/Structure/6'>two domains.</scene>
PTEN is a tumor suppressor protein that is mutated in several human cancersThese 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 intereact with the membrane.  The phosphatase section (blue) interacts with the ligand and the phosphate head.  These interactions are controled by two separate loops, the P-loop and the "TI" loop.


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

Revision as of 00:14, 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 intereact with the membrane. The phosphatase section (blue) interacts with the ligand and the phosphate head. These interactions are controled by two separate loops, the P-loop and the "TI" loop.

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