Extended Data Fig. 5: CCP5 tail binding interface is highly conserved among CCP5 but variable compared to CCP1. | Nature

Extended Data Fig. 5: CCP5 tail binding interface is highly conserved among CCP5 but variable compared to CCP1.

From: Tubulin code eraser CCP5 binds branch glutamates by substrate deformation

Extended Data Fig. 5

a. CCP5 molecular surface color-coded based on sequence identity among CCP5 (Supplementary Fig. 4). b. CCP5 surface color-coded based on sequence identity among human, mouse, zebrafish, Chlamydomonas and Tetrahymena CCP5 and CCP1. c. Close-up view of the tubulin tail binding interface showing high conservation between CCP1 and 5 for scissile branch glutamate recognition and a non-conserved molecular surface for tubulin tail binding.

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