Molecular Playground/TRAIL

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One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.


Drag the structure with the mouse to rotate

Molecular Playground Banner: TRAIL, a novel cancer therapeutic

TRAIL, or tumor-necrosis factor apoptosis-inducing ligand, is a member of the TNF superfamily that has attracted attention for its specificity towards cancer cells with limited toxicity towards most normal cells. TRAIL is a type II transmembrane protein with an extracellular domain that can be proteolyticly cleaved, and which forms a homotrimer that binds three monomeric death receptors (DRs). It binds to DR4 and DR5, which elicit signal transduction of caspase-8 mediated apoptosis via the death receptor pathway, or it can bind to the decoy receptors (DcR1, DcR2, or osteoprotegerin) which have truncated or non-functional intracellular death domains. Receptor binding by TNFα can stimulate both pro-apoptotic signals (via caspase-8) and anti-apoptotic signals (via NFκB). However, TRAIL has attenuated induction of NFκB, leading to a pronounced death signal via a p53-independent mechanism. In addition, the antagonistic decoy receptors are widely-expressed in normal tissues and confer a resistance to TRAIL-mediated apoptosis.

This scene shows only the extracellular domain of TRAIL. Each beta-sheet is shown in a different color and the bright green loop designates the section of the protein which is responsible for binding with the various death receptors.

3D structures of TRAIL


Proteopedia Page Contributors and Editors (what is this?)

Charles Swofford, Michal Harel, David Griffin, Lynmarie K Thompson

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