PTEN

This is a placeholderThis is a placeholder

This is a placeholder text to help you get started in placing a Jmol applet on your page. At any time, click "Show Preview" at the bottom of this page to see how it goes.

Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load and display another structure.

spinqualitylabelsall models PDB ID 1d5r Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1d5r, resolution 2.10Å ()
Ligands:
Activity:	Protein-tyrosine-phosphatase, with EC number 3.1.3.48
Structural annotation: Resources: CATH : 1D5Ra02, 1D5Ra01 InterPro : Ipr014020, Ipr000340, Ipr000387, Ipr008973, Ipr000242, Ipr014019 Pfam : PF00782 SCOP : d1d5ra1, d1d5ra2 UniProt : P60484
Functional annotation: Cellular component: cytoplasm Biological process: phosphoinositide dephosphorylation induction of apoptosis cardiac muscle development cell migration heart development angiogenesis negative regulation of cell cycle regulation of protein stability dephosphorylation inositol phosphate dephosphorylation negative regulation of apoptosis cell cycle negative regulation of protein kinase B signaling cascade central nervous system development lipid metabolic process negative regulation of focal adhesion formation endothelial cell migration regulation of cyclin-dependent protein kinase activity cell proliferation negative regulation of cell migration protein amino acid dephosphorylation negative regulation of cell proliferation Molecular function: protein binding phosphoric monoester hydrolase activity lipid binding inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity PDZ domain binding protein tyrosine/serine/threonine phosphatase activity phosphoprotein phosphatase activity phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity hydrolase activity phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity protein tyrosine phosphatase activity protein serine/threonine phosphatase activity phosphatidylinositol-3-phosphatase activity
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
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 , which decrease the protein's activity from 50-60%. The "TI" loop also contain mutations. These include mutations of 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. In addition to the active loops in the phosphatase domain, the C2 domain also contains mutations that affect the protein's ability to interact with the membrane. This mutation is located at the which is mutated to a Gln. There are several mutations located along some of the general portions of the protein. The most influencial of of these is the mutation of to Ala. This mutation alone causes a 700-fold reduction in the protein's catalytic activity.