Abscisic acid (ABA) plays a vital role in many developmental processes and the response to adaptive stress in plants.Under drought stress, plants enhance levels of ABA and activate ABA receptors, but under harsh environmental stress, plants usually cannot efficiently synthesize and release sufficient quantities of ABA. The response of plants to harsh environmental stress may be improved through ABA-independent activation of ABA receptors. The molecular basis of ABA-independent inhibition of group A protein phosphatasestype 2C (PP2Cs) by PYR1/PYLs is not yet clear. Here, we used our previously reported structures of PYL3 to first obtain the monomeric PYL3 mutant and then introduce bulky hydrophobic residue substitutions to promote the closure of the Gate/L6/CL2 loop, thereby mimicking the conformation of ABA occupancy. Through structure-guided mutagenesis and biochemical characterization, we investigated the
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