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TRAIL (TNF-RELATED APOPTOSIS INDUCING LIGAND)TRAIL (TNF-RELATED APOPTOSIS INDUCING LIGAND)
Name: Marissa McGarry 03/02/09
The overall structure of TRAIL is a set of 13 (shown in red). As you can see, the exterior of the protein has all of the side chains, as shown in pink.
, shown in green, is a hydrophobic element on the surface of the protein.
TRAIL to the tumor necrosis factor(TNF) family. TRAIL selectively induces apoptosis in a wide variety of tumor cells but not in normal cells, which gives it promise as a cancer therapeutic.
"To help in elucidating its biological roles and designing mutants with improved therapeutic potential, we have determined the crystal structure of human TRAIL. The structure reveals that a unique frame insertion of 12-16 amino acids adopts a salient loop structure penetrating into the receptor-binding site. The loop drastically alters the common receptor-binding surface of the TNF family most likely for the specific recognition of cognate partners. A structure-based mutagenesis study demonstrates a critical role of the insertion loop in the cytotoxic activity of TRAIL."
Reference: 1d2q proteopedia page
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| 1d2q, resolution 2.80Å () | |||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
