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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Domain III of calpain is a ca2+-regulated phospholipid-binding domain.

The X-ray structure of m-calpain shows that domain III of the large subunit is structurally related to C2 domains, Ca2+-regulated lipid binding modules in many enzymes. To address whether this structural similarity entails functional analogy, we have characterized recombinant domain III from rat micro- and m-calpain and Drosophila CALPB. In a Ca2+ overlay assay domain III displays a large capacity for Ca2+ binding, commensurable with that of domain IV, the principal Ca2+-binding domain of calpains. The amount of Ca2+ bound to domain III increases 2- to 10-fold upon the addition of liposomes containing 20-40% di- and triphosphoinositides. Conversely, phospholipid-binding in spin-column size-exclusion chromatography is significantly promoted by Ca2+, in a manner similar to known C2 domains. These results suggest that domain III might be the primary lipid binding site of calpain and may play a decisive role in orchestrating Ca2+- and lipid activation of the enzyme.[1]

References

  1. Domain III of calpain is a ca2+-regulated phospholipid-binding domain. Tompa, P., Emori, Y., Sorimachi, H., Suzuki, K., Friedrich, P. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
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