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. Author manuscript; available in PMC: 2015 Feb 19.
Published in final edited form as: Science. 2014 Jul 25;345(6195):459–463. doi: 10.1126/science.1254836

Fig. 3. The ‘open’, activated form of AP2 is not compatible with the β2 hinge binding back into the core.

Fig. 3

Release of the clathrin-binding motif stimulated by conformational change. Top panels: ‘locked’AP2 core, in solution or transiently bound to the plasma membrane via PtdIns(4,5)P2 (left) and ‘open’ AP2 stably attached to the membrane via multiple PtdIns(4,5)P2s and cargo. Lower panels: views of the hinge binding site in each conformational state; in the ‘open’ state (right), the hinge residues from the ‘locked’ state βhingeH6.AP2 structure are superposed onto the ‘open’ structure and shown in grey.