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A Gate-Latch-Lock Mechanism for Hormone Signaling by Abscisic Acid Receptors
TLDR
Crystal structures of apo and ABA-bound receptors as well as a ternary PYL2–ABA–PP2C complex are reported to identify a conserved gate–latch–lock mechanism underlying ABA signalling.
Structural Basis of CXCR4 Sulfotyrosine Recognition by the Chemokine SDF-1/CXCL12
TLDR
The nuclear magnetic resonance structure of a constitutively dimeric SDF-1 in complex with a CXCR4 fragment that contains three sulfotyrosine residues important for a high-affinity ligand-receptor interaction is reported.
Activation of dimeric ABA receptors elicits guard cell closure, ABA-regulated gene expression, and drought tolerance
TLDR
The effects of quinabactin are sufficiently similar to those of ABA that it is able to rescue multiple phenotypes observed in the ABA-deficient mutant aba2 and define the dimeric receptors as key targets for chemical modulation of vegetative ABA responses.
Interconversion between two unrelated protein folds in the lymphotactin native state
TLDR
The results demonstrate that the functional repertoire and regulation of a single naturally occurring amino acid sequence can be expanded by access to a set of highly dissimilar native-state structures.
Multiple WASP-interacting Protein Recognition Motifs Are Required for a Functional Interaction with N-WASP*
TLDR
The present results show that, when combined, the WIP-(451-485) sequence wraps further around the EVH1 domain, extending the interface observed previously, and demonstrating a functional requirement for the entire binding domain, which is significantly longer than the polyproline motifs recognized by other EVH 1 domains.
The monomer–dimer equilibrium of stromal cell‐derived factor‐1 (CXCL 12) is altered by pH, phosphate, sulfate, and heparin
TLDR
It is demonstrated that SDF1 can form a dimeric structure in solution, but only at nonacidic pH when stabilizing counterions are present, and this pH‐sensitive aggregation behavior is explained by a dense cluster of positively charged residues at the SDF 1 dimer interface.
Structural basis for selective activation of ABA receptors
TLDR
It is shown that subtle differences between receptor binding pockets control ligand orientation between productive and nonproductive modes and this provides a robust framework for the design of new agonists and reveals a new mechanism for agonist selectivity.
Potent and selective activation of abscisic acid receptors in vivo by mutational stabilization of their agonist-bound conformation
TLDR
The results set the stage for systematic gain-of-function studies of PYR1 and related ABA receptors and reveal that, despite the large number of receptors, activation of a single receptor is sufficient to activate signaling in planta.
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