图2. ABA诱导的受体构象变化（引自CUTLER等^[12]）
在ABA缺乏时,PYR/PYL（pyrabactin resistance 1/pyrabactin resistance 1-like）蛋白具有一个开放的门和门闩环的构型（分别为红色和绿色）,它们位于ABA结合口袋的侧面。ABA的结合诱导门和门闩的关闭,依次产生相互作用的表面,使2C类蛋白磷酸酶（PP2C）对接到结合ABA的受体上。门中的一个保守的脯氨酸（对应于PYR1中的脯氨酸88残基,用蓝色表示）在对接位点与PP2C形成直接的接触,这解释了用PYR1^P88观察到的PP2C结合的缺陷

Fig. 2. ABA-induced changes in receptor conformation (From CUTLER et al.^[12])
In the absence of ABA, PYR/PYL (pyrabactin resistance 1/pyrabactin resistance 1-like) proteins possess an open conformation of the gate and latch loops (red and green, respectively) that flank the ABA-binding pocket. Binding of ABA induces closure of the gate and latch, which in turn creates the interaction surface that recruits docking of type 2C protein phosphatases (PP2C) onto the ABA-bound receptors. A conserved proline in the gate (which corresponds to the residue to proline 88 in PYR1 and is shown in blue) forms a direct contact with the PP2C at the docking site, which explains the PP2C-binding defect observed with PYR1^P88