Natural Full Color Nylon 12 (MJF)
Apaf-1 Caspase 9 5WVE
Made by
Print With Shapeways
Choose Your Size
Choose Your Material
Choose your color and finish
Choose Your Size
$72.76
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 Apaf-1 Caspase 9 is visualized as a volumetric surface and colored to visualize each chain uniquely. This 3D protein model was created from PDB ID: 5WVE.
Protein Description
Mammalian intrinsic apoptosis requires activation of the initiator caspase-9, which then cleaves and activates the effector caspases to execute cell killing. The heptameric Apaf-1 apoptosome is indispensable for caspase-9 activation by together forming a holoenzyme. The molecular mechanism of caspase-9 activation remains largely enigmatic. Here, we report the cryoelectron microscopy (cryo-EM) structure of an apoptotic holoenzyme and structure-guided biochemical analyses. The caspase recruitment domains (CARDs) of Apaf-1 and caspase-9 assemble in two different ways: a 4:4 complex docks onto the central hub of the apoptosome, and a 2:1 complex binds the periphery of the central hub. The interface between the CARD complex and the central hub is required for caspase-9 activation within the holoenzyme. Unexpectedly, the CARD of free caspase-9 strongly inhibits its proteolytic activity. These structural and biochemical findings demonstrate that the apoptosome activates caspase-9 at least in part through sequestration of the inhibitory CARD domain.
This 3D printed protein model of Apaf-1 Caspase 9 is visualized as a volumetric surface and colored to visualize each chain uniquely. This 3D protein model was created from PDB ID: 5WVE.
Protein Description
Mammalian intrinsic apoptosis requires activation of the initiator caspase-9, which then cleaves and activates the effector caspases to execute cell killing. The heptameric Apaf-1 apoptosome is indispensable for caspase-9 activation by together forming a holoenzyme. The molecular mechanism of caspase-9 activation remains largely enigmatic. Here, we report the cryoelectron microscopy (cryo-EM) structure of an apoptotic holoenzyme and structure-guided biochemical analyses. The caspase recruitment domains (CARDs) of Apaf-1 and caspase-9 assemble in two different ways: a 4:4 complex docks onto the central hub of the apoptosome, and a 2:1 complex binds the periphery of the central hub. The interface between the CARD complex and the central hub is required for caspase-9 activation within the holoenzyme. Unexpectedly, the CARD of free caspase-9 strongly inhibits its proteolytic activity. These structural and biochemical findings demonstrate that the apoptosome activates caspase-9 at least in part through sequestration of the inhibitory CARD domain.
Details
What's in the box:
sml_5WVE_Apaf-1-Caspase-9_max_x100-8cm_v7
Dimensions:
Success Rate:
First To try.
What's this?
Rating:
Mature audiences only.
