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From Proteopedia
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Calpains 1 and 2 are heterodimeric proteases in which large (relative molecular mass M(r) 80000) and small (M(r) 28000) subunits are linked through their respective PEF (penta-EF-hand) domains. The skeletal muscle-specific calpain 3 is believed not to form a heterodimer with the small subunit but might homodimerize through its PEF domain. Size-exclusion chromatography and analytical ultracentrifugation of the recombinant PEF domain of calpain 3 show that it forms a stable homodimer that does not dissociate on dilution. Molecular modelling suggests that there would be no barriers to the dimerization of the whole enzyme through the PEF domains. This orientation would place the catalytic centres at opposite ends of the dimer.
Homodimerization of calpain 3 penta-EF-hand domain.,Ravulapalli R, Diaz BG, Campbell RL, Davies PL Biochem J. 2005 Jun 1;388(Pt 2):585-91. PMID:15660530[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Ravulapalli R, Diaz BG, Campbell RL, Davies PL. Homodimerization of calpain 3 penta-EF-hand domain. Biochem J. 2005 Jun 1;388(Pt 2):585-91. PMID:15660530 doi:10.1042/BJ20041821
