PYR1 Antibody

1. study suggests both nuclear and cytoplasmic PYR1 participate in the control of ABA signal transduction PMID: 28109881
2. The transgenic plants show an acute abscisic acid (ABA) insensitivity, demonstrating the importance of ABA-mediated PYR/PYL/RCAR-PP2C contacts for receptor function in vivo. PMID: 21357183
3. Pyr1 receptor contributes to ozone, reduced air humidity and darkness induced stomatal regulation. PMID: 23703845
4. findings are generally consistent with the competitive-interaction model for PYR1 but highlight dynamical contributions of the PYR1 structure in mediating interaction selectivity PMID: 23825939
5. This work illustrates how oligomerization of abscisic acid receptors can modulate hormonal responses in Arabidopsis and more generally, the sensitivity of a ligand-dependent signalling system. PMID: 21847091
6. Subtle changes in the binding pockets of PYR/PYL proteins control ligand orientation inside the pocket, and this is sufficient to explain whether pyrabactin acts as an effective receptor agonist. [PYR1] PMID: 20729860
7. X-ray data is reported for PYL9/RCAR1, PYL5/RCAR8 and PYR1/RCAR11 in the presence of (+)-abscisic acid. The three proteins crystallize in space groups P3(1)21/P3(2)21, P2 and P1, respectively. X-ray intensity data were collected to 1.9-2.6 A resolution. PMID: 20383021
8. findings show that abscissic binds to PYRABACTIN RESISTANCE 1 (PYR1),At4g17870, which in turn binds to and inhibits Type 2C protein phosphatases (HAB1) PMID: 19407142
9. the crystal structure of Arabidopsis thaliana PYR1, which consists of a dimer in which one of the subunits is bound to ABA. PMID: 19898494
10. structure of pyrabactin resistance 1 (PYR1); structure reveals an alpha/beta helix-grip fold & homodimeric assembly; abscisic acid (ABA) binding within a large internal cavity switches structural motifs distinguishing ABA-free from ABA-bound conformations PMID: 19933100

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KEGG: ath:AT4G17870

STRING: 3702.AT4G17870.1

UniGene: At.2045