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3NJO

X-ray crystal structure of the Pyr1-pyrabactin A complex

3NJO の概要
エントリーDOI10.2210/pdb3njo/pdb
関連するPDBエントリー3NJ0 3NJ1
分子名称Abscisic acid receptor PYR1, 4-bromo-N-(pyridin-2-ylmethyl)naphthalene-1-sulfonamide, SULFATE ION, ... (7 entities in total)
機能のキーワードstart, aba, pyr/pyl/rcar, plant hormone, structural genomics, protein structure initiative, psi, center for eukaryotic structural genomics, cesg, hormone receptor
由来する生物種Arabidopsis thaliana (thale-cress)
細胞内の位置Cytoplasm : O49686
タンパク質・核酸の鎖数3
化学式量合計66929.90
構造登録者
主引用文献Peterson, F.C.,Burgie, E.S.,Park, S.Y.,Jensen, D.R.,Weiner, J.J.,Bingman, C.A.,Chang, C.E.,Cutler, S.R.,Phillips, G.N.,Volkman, B.F.
Structural basis for selective activation of ABA receptors.
Nat.Struct.Mol.Biol., 17:1109-1113, 2010
Cited by
PubMed Abstract: Changing environmental conditions and lessening fresh water supplies have sparked intense interest in understanding and manipulating abscisic acid (ABA) signaling, which controls adaptive responses to drought and other abiotic stressors. We recently discovered a selective ABA agonist, pyrabactin, and used it to discover its primary target PYR1, the founding member of the PYR/PYL family of soluble ABA receptors. To understand pyrabactin's selectivity, we have taken a combined structural, chemical and genetic approach. We show that subtle differences between receptor binding pockets control ligand orientation between productive and nonproductive modes. Nonproductive binding occurs without gate closure and prevents receptor activation. Observations in solution show that these orientations are in rapid equilibrium that can be shifted by mutations to control maximal agonist activity. Our results provide a robust framework for the design of new agonists and reveal a new mechanism for agonist selectivity.
PubMed: 20729860
DOI: 10.1038/nsmb.1898
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.473 Å)
構造検証レポート
Validation report summary of 3njo
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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