CARD (domain)
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CARD (domain)
Caspase recruitment domains, or caspase activation and recruitment domains (CARDs), are Short linear motif, interaction motifs found in a wide array of proteins, typically those involved in processes relating to inflammation and apoptosis. These domains mediate the formation of larger protein complexes via direct interactions between individual CARDs. CARDs are found on a strikingly wide range of proteins, including helicases, kinases, mitochondrial proteins, caspases, and other cytoplasmic factors. Basic features CARDs are a subclass of protein motif known as the death fold, which features an arrangement of six to seven antiparallel alpha helices with a hydrophobic core and an outer face composed of charged residues. Other motifs in this class include the pyrin domain (PYD), death domain (DD), and death effector domain (DED), all of which also function primarily in regulation of apoptosis and inflammatory responses. In apoptosis CARDs were originally characterized based on th ...
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Short Linear Motif
In molecular biology short linear motifs (SLiMs), linear motifs or minimotifs are short stretches of protein primary structure, protein sequence that mediate protein–protein interaction. The first definition was given by Tim Hunt: "The sequences of many proteins contain short, conserved motifs that are involved in recognition and targeting activities, often separate from other functional properties of the molecule in which they occur. These motifs are linear, in the sense that three-dimensional organization is not required to bring distant segments of the molecule together to make the recognizable unit. The conservation of these motifs varies: some are highly conserved while others, for example, allow substitutions that retain only a certain pattern of charge across the motif." Attributes SLiMs are generally situated in Intrinsically unstructured proteins, intrinsically disordered regions (over 80% of known SLiMs), however, upon interaction with a structured partner secondary ...
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