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. Author manuscript; available in PMC: 2018 Sep 1.
Published in final edited form as: Traffic. 2017 Sep;18(9):590–603. doi: 10.1111/tra.12499

Figure 3. Structural and functional comparison of epsin1 and tepsin ENTH domains.

Figure 3

(A) Overlay of epsin1 ENTH (yellow; PDB: 1H0A) and tENTH (green) domains. Tepsin lacks the amphipathic helix0 found in other ENTHs and instead contains an elongated helix1. (B) Equivalent electrostatic surface views of epsin1 ENTH (left) and tENTH (right). Epsin1 contains a basic binding pocket to accommodate a phosphoinositide head group, while tepsin lacks this binding pocket because of the absence of helix0. Biochemical data using recombinant ENTH domains on PIP strips confirms the structural predictions that epsin1 ENTH recognizes phosphoinositides, while tepsin ENTH does not.