Glossy Full Color Sandstone
PTEN Tumor Supressor 1D5R
Made by
Print With Shapeways
Choose Your Size
Choose Your Material
Choose your color and finish
Choose Your Size
$50.84
Choose Your Material
Choose your color and finish
Have a question about this product?
contact the designerYou must be logged in and verified to contact the designer.
Product Description
Model Description
This 3D printed protein model of PTEN Tumor Suppressor is visualized as a volumetric surface and colored by the protein's bFactor. This 3D printed protein model was created from PDB ID: 1D5R
Protein Description
The PTEN tumor suppressor is mutated in diverse human cancers and in hereditary cancer predisposition syndromes. PTEN is a phosphatase that can act on both polypeptide and phosphoinositide substrates in vitro. The PTEN structure reveals a phosphatase domain that is similar to protein phosphatases but has an enlarged active site important for the accommodation of the phosphoinositide substrate. The structure also reveals that PTEN has a C2 domain. The PTEN C2 domain binds phospholipid membranes in vitro, and mutation of basic residues that could mediate this reduces PTEN's membrane affinity and its ability to suppress the growth of glioblastoma tumor cells. The phosphatase and C2 domains associate across an extensive interface, suggesting that the C2 domain may serve to productively position the catalytic domain on the membrane.
This 3D printed protein model of PTEN Tumor Suppressor is visualized as a volumetric surface and colored by the protein's bFactor. This 3D printed protein model was created from PDB ID: 1D5R
Protein Description
The PTEN tumor suppressor is mutated in diverse human cancers and in hereditary cancer predisposition syndromes. PTEN is a phosphatase that can act on both polypeptide and phosphoinositide substrates in vitro. The PTEN structure reveals a phosphatase domain that is similar to protein phosphatases but has an enlarged active site important for the accommodation of the phosphoinositide substrate. The structure also reveals that PTEN has a C2 domain. The PTEN C2 domain binds phospholipid membranes in vitro, and mutation of basic residues that could mediate this reduces PTEN's membrane affinity and its ability to suppress the growth of glioblastoma tumor cells. The phosphatase and C2 domains associate across an extensive interface, suggesting that the C2 domain may serve to productively position the catalytic domain on the membrane.
Details
What's in the box:
Sml: PTEN_rumorSupressor_1D5R
Dimensions:
Success Rate:
First To try.
What's this?
Rating:
Mature audiences only.
