Maurocalcine

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Structures	Swiss-model
Domains	InterPro

Maurocalcine
	Structure of Maurocalcine, determined by NMR
Identifiers
Organism	Scorpio maurus palmatus
Symbol	MCa
PDB	1c6w
UniProt	P60254
Search for
Structures	Swiss-model
Domains	InterPro

Maurocalcine is a protein isolated from the venom of the scorpion Maurus palmatus, which belongs to the family Chactidae. It was first reported by Fajloun et al. in 2000.[1]

It is 33 Amino acid residues in length, containing three disulphide bonds which folds into the inhibitor cystine knot motif.[2] It acts by modifying the activity of the type 1 ryanodine receptor.[1]

References

Fajloun Z, Kharrat R, Chen L, Lecomte C, Di Luccio E, Bichet D, El Ayeb M, Rochat H, Allen PD, Pessah IN, De Waard M, Sabatier JM (March 2000). "Chemical synthesis and characterization of maurocalcine, a scorpion toxin that activates Ca(2+) release channel/ryanodine receptors". FEBS Letters. 469 (2–3): 179–85. doi:10.1016/S0014-5793(00)01239-4. PMID 10713267.
Mosbah A, Kharrat R, Fajloun Z, Renisio JG, Blanc E, Sabatier JM, El Ayeb M, Darbon H (August 2000). "A new fold in the scorpion toxin family, associated with an activity on a ryanodine-sensitive calcium channel". Proteins. 40 (3): 436–42. doi:10.1002/1097-0134(20000815)40:3<436::AID-PROT90>3.0.CO;2-9. PMID 10861934.

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[synth-1] Fajloun Z, Kharrat R, Chen L, Lecomte C, Di Luccio E, Bichet D, El Ayeb M, Rochat H, Allen PD, Pessah IN, De Waard M, Sabatier JM (March 2000). "Chemical synthesis and characterization of maurocalcine, a scorpion toxin that activates Ca(2+) release channel/ryanodine receptors". FEBS Letters. 469 (2–3): 179–85. doi:10.1016/S0014-5793(00)01239-4. PMID 10713267.

[2] Mosbah A, Kharrat R, Fajloun Z, Renisio JG, Blanc E, Sabatier JM, El Ayeb M, Darbon H (August 2000). "A new fold in the scorpion toxin family, associated with an activity on a ryanodine-sensitive calcium channel". Proteins. 40 (3): 436–42. doi:10.1002/1097-0134(20000815)40:3<436::AID-PROT90>3.0.CO;2-9. PMID 10861934.