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ankyrin repeat domain-containing protein
ankyrin repeat protein
Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity [2][3]. [1]. 2141669. Hereditary spherocytosis associated with deletion of human erythrocyte ankyrin gene on chromosome 8. Lux SE, John KM, Bennett V;. Nature 1990;345:736-739. [2]. 12456646. Crystal structure of a 12 ANK repeat stack from human ankyrinR. Michaely P, Tomchick DR, Machius M, Anderson RG;. EMBO J. 2002;21:6387-6396. [3]. 14731966. The ANK repeat: a ubiquitous motif involved in macromolecular recognition. Michaely P, Bennett V;. Trends Cell Biol. 1992;2:127-129. (from Pfam)
ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions
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