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Recently crystal structure of large part of PKC βII (C1B, C2, and catalytic domain) was reported, and interesting activation mechanism was also proposed. In this structure, it was indicated that C1B domain would be surrounded by C1A, C2, and catalytic domain. See
-
Recently crystal structure of large part of PKC βII (C1B, C2, and catalytic domain) was reported, and interesting activation mechanism was also proposed. In this structure, it was indicated that C1B domain would be surrounded by C1A, C2, and catalytic domain. See: Leonard, T. A.; Różycki, B.; Saidi, L. F.; Hummer, G.; Hurley, J. H. Cell 2011, 144, 55-66.
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note
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As far as we know, there is no direct method to estimate the binding affinity toward C1A domain using whole PKCα.
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