Molecular Playground/TRAIL: Difference between revisions
New page: <applet size='[450,338]' frame='true' align='right' caption='YYY' /> <scene name='User:Charles_Swofford/Sandbox_1/1/21'>TRAIL</scene> TRAIL, or tumor-necrosis factor apoptosis-inducing l... |
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One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground]. | |||
<applet size='[450,338]' frame='true' align='right' | <applet size='[450,338]' frame='true' align='right' | ||
caption=' | caption='TRAIL' /> | ||
<scene name='User:Charles_Swofford/Sandbox_1/1/21'>TRAIL</scene> | <scene name='User:Charles_Swofford/Sandbox_1/1/21'>TRAIL</scene> | ||
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. | 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. | 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== | |||
[[TRAIL]] | |||
Latest revision as of 16:54, 30 January 2012
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.
|
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.