Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains.
Nature (2008)
Crystal structures of calpain-E64 and -leupeptin inhibitor complexes reveal mobile loops gating the active site
J.Mol.Biol. (2004)
Calpain silencing by a reversible intrinsic mechanism
Nat.Struct.Mol.Biol. (2003)
;A structural model for the inhibition of calpain by calpastatin: crystal structures of the native domain VI of calpain and its complexes with calpastatin peptide and a small molecule inhibitor
;
J.Mol.Biol. (2003)
A Ca(2+) switch aligns the active site of calpain
Cell(Cambridge,Mass.) (2002)
The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium
Proc.Natl.Acad.Sci.USA (2000)
;Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation
;
Embo J. (1999)