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![[Figure 1]](ba5238fig1mag.jpg)
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Figure 1
(a) Schematic representation of the AP2 clathrin adaptor. The `core' is indicated; the α and β2 hinge and appendage subdomains are shown in paler colours to indicate the fact that they do not form part of the core. Note that μ2 is composed of an N-terminal longin-fold subdomain and a C-terminal `μ-homology' subdomain. (b) Schematics of the AP2 constructs used to express recombinant AP2 core in E. coli, showing the C-terminally GST-tagged α trunk subdomain, the N-terminally hexahistidine-tagged β2 trunk subdomain and the μ2 and σ2 subunits. (c) Conformational states of the AP2 core. `Locked' AP2 (PDB entry 2vgl ; Collins et al., 2002  ) is unable to bind cargo owing to steric blockage of the binding sites by the β2 subunit. Upon plasma-membrane recruitment [driven by association with PtdIns(4,5)P2], the complex undergoes a conformational change that reveals the cargo-binding sites, allowing cargo recruitment and stabilization of the `open' conformation (PDB entry 2xa7
; Jackson et al., 2010). |
![[Figure 1]](ba5238fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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