Global InformationMaurocalcine information
| Maurocalcine | |||||||
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 Structure of Maurocalcine, determined by NMR | |||||||
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| Organism | |||||||
| Symbol | MCa | ||||||
| PDB | 1c6w | ||||||
| UniProt | P60254 | ||||||
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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.[1] 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.[1]
- ^ a b Fajloun Z, Kharrat R, Chen L, Lecomte C, Di Luccio E, Bichet D, et al. (March 2000). "Chemical synthesis and characterization of maurocalcine, a scorpion toxin that activates Ca(2+) release channel/ryanodine receptors". FEBS Letters. 469 (2–3): 179–185. doi:10.1016/S0014-5793(00)01239-4. PMID 10713267. S2CID 41435933.