2L2N
Backbone 1H, 13C, and 15N Chemical Shift Assignments for the first dsRBD of protein HYL1
2L2N の概要
| エントリーDOI | 10.2210/pdb2l2n/pdb |
| 関連するPDBエントリー | 2L2M |
| NMR情報 | BMRB: 17143 |
| 分子名称 | Hyponastic leave 1 (1 entity in total) |
| 機能のキーワード | dsrbd, mirna, rna binding protein, plant protein |
| 由来する生物種 | Arabidopsis thaliana (mouse-ear cress,thale-cress) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 11385.82 |
| 構造登録者 | Rasia, R.M.,Mateos, J.L.,Bologna, N.G.,Burdisso, P.,Imbert, L.,Palatnik, J.F.,Boisbouvier, J. (登録日: 2010-08-23, 公開日: 2010-09-29, 最終更新日: 2024-05-01) |
| 主引用文献 | Rasia, R.M.,Mateos, J.,Bologna, N.G.,Burdisso, P.,Imbert, L.,Palatnik, J.F.,Boisbouvier, J. Structure and RNA Interactions of the Plant MicroRNA Processing-Associated Protein HYL1. Biochemistry, 49:8237-8239, 2010 Cited by PubMed Abstract: HYL1 is a double-stranded RNA binding protein involved in microRNA processing in plants. HYL1 enhances the efficiency and precision of the RNase III protein DCL1 and participates in microRNA strand selection. In this work, we dissect the contributions of the domains of HYL1 to the binding of RNA targets. We found that the first domain is the main contributor to RNA binding. Mapping of the interaction regions by nuclear magnetic resonance on the structure of HYL1 RNA-binding domains showed that the difference in binding capabilities can be traced to sequence divergence in β2-β3 loop. The possible role of each domain is discussed in light of previous experimental data. PubMed: 20735118DOI: 10.1021/bi100672x 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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