Maurocalcine

Protein

Maurocalcine (MCa) is a protein, 33 Amino acid residues in length, isolated from the venom of the scorpion Maurus palmatus, which belongs to the family Chactidae, first characterized in 2000. The toxin is present in such small amounts that it could not be isolated to analyze it, so a chemical synthesis of this toxin was performed by the solid-phase technique so it could be fully characterized. It shares 82% sequence identity with imperatoxin A (IpTx A), a scorpion toxin from the venom of Pandinus imperator. IpTx A acts by modifying the activity of the type 1 ryanodine receptor of skeletal muscle. RyR controls the intracellular Ca2+ permeability of various cell types and is central in the process of excitation–contraction of muscle tissues. The synthesized toxin, sMCa is active on RyR1 and it binds onto a site different from that of ryanodine itself.

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