About CARD / Caspase Recruitment Domain Family:
CARD is an interactive protein belonging to the death domain superfamily.
The DD superfamily is among the most prominent families of the interactive protein modules and comprises the death domain, death effector domain, and pyrin domain. CARD gets used in the inflammation and apoptosis processes.
The DD subfamily uses proteases as a precursor of the nucleated cells. It also utilizes the two-step signaling pathway. CARD uses different mechanisms to convert the apoptotic stimuli to proteolytic activity.
These activities are then responsible for multiplying the prostrate substrate proteolysis for efficient apoptosis.
Caspase Recruitment Domain Family Interactions
Activation of the caspase-9, which was the first structure to exhibit the DD protein interaction interface, requires a specific assembly by the apoptosome. Its result is complex CARD-CARD heterodimeric structures. Consequently, different dimeric forms are stemming from the initial setup, thus enhancing its functionality.
The subfamily domains' primary function is to monitor and regulate the inflammation and apoptosis processes in mammals. Typically, the inflammation is due to bacterial or viral infections. It is also responsive to some types of stress signals.
Collectively, CARD domains work to illuminate the autoimmune system. Having a deficiency in CARD proteins can cause you a dip in your immunodeficiency – further elaborating its role in the immune system.
Caspase Recruitment Domain Family Structure
You can find the CARD domain in various proteins like mitochondrial proteins, helicases, or kinases. The most common type is the six-helix structure (a conservative bundle fold), a significant component in your immune response system.
The CARD family's complex oligomeric structure is a recent entry in the CARD family due to recent research of the RIG-I and MAVS complex.
CARD plays a significant role in your responsiveness to various stimuli and inflammations.