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Literature summary for 3.4.22.54 extracted from

  • Ye, Q.; Campbell, R.L.; Davies, P.L.
    Structures of human calpain-3 protease core with and without bound inhibitor reveal mechanisms of calpain activation (2018), J. Biol. Chem., 293, 4056-4070 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor diffusion method at 22°C, structures of calpain-3 Protease core mutant-C129S, calpain-3 protease core in complex with E-64, calpain-3 protease core in complex with leupeptin Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
E-64
-
Homo sapiens
leupeptin
-
Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P20807
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification insertion sequence IS1 interrupts the protease core and must be cleaved for activation and substrate binding Homo sapiens

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
Homo sapiens
-

Subunits

Subunits Comment Organism
homodimer
-
Homo sapiens

General Information

General Information Comment Organism
malfunction limb-girdle muscular dystrophy type 2a arises from mutations in the Ca+-activated intracellular cysteine protease calpain-3 Homo sapiens