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. Author manuscript; available in PMC: 2021 Jul 16.
Published in final edited form as: Adv Exp Med Biol. 2019;1111:77–137. doi: 10.1007/5584_2018_288

Figure 3.

Figure 3.

PPIn-binding domains associated with the generation or recognition of membrane curvature. A comparison of the different PPIn-binding modes used by the membrane deforming ENTH (a; epsin ENTH bound to Ins(1,4,5)P3; PDB entry 1H0A) and ANTH (b; N-terminal domain of CALM bound to PtdIns(4,5)P2; PDB entry 1HFA) domains. The unstructured α0 helix that becomes structured upon interactions with targeted PPIn lipids, typically PtdIns(4,5)P2, is highlighted by blue. The canonical N-BAR domain of amphyphysin (c; PDB entry 1URU) is shown as the activate homodimer. For further details about each of these domains, please refer to Section 5.8 of the text. Prepared using the PyMOL Molecular Graphics System, Version 2.0 Schrödinger, LLC.