Biochemical and Biophysical Research Communications
Regular ArticleModulation of the Calpain Autoproteolysis by Calpastatin and Phospholipids
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2016, Progress in NeurobiologyCitation Excerpt :The CBSW domain was formerly referred to as domain III or C2L domain because it is composed of eight anti-parallel β-strands that resemble the C2 domain found in other proteins, such as protein kinase C (PKC) and phospholipase C (PLC); however it was recently renamed CBSW because in its 3D structure this domain is not similar to the C2 domain. The CBSW domain was proposed to interact with Ca2+ and phospholipids (Corbalan-Garcia and Gomez-Fernandez, 2010; Tompa et al., 2001; Vines, 2012) and, accordingly, phospholipids were shown to increase the Ca2+ sensitivity of calpains (Melloni et al., 1996; Tompa et al., 2001). However, different studies showed that the cation does not interact with this region in the crystal structures of Ca2+-bound calpain complexed with calpastatin (Hanna et al., 2008; Moldoveanu et al., 2008).
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