Department of Biology, Indian Institute of Science Education and Research (IISER), Tirupati, Andhra Pradesh 517507, India.
Department of Statistics/Bioinformatics, Rajendra Memorial Research Institute of Medical Sciences, ICMR, Agamkuan, Patna 800007, India.
Int J Biol Macromol. 2021 Oct 31;189:965-979. doi: 10.1016/j.ijbiomac.2021.08.152. Epub 2021 Aug 24.
Plasma membrane-bound receptor proteins play crucial roles in the perception and further transmission of regulatory signals to modulate numerous developmental and metabolic events. Precise functioning and fine-tuning of Nod factor receptor (NFR) mediated signalling is a critical requirement for root nodule symbiosis. Here, we have identified, cloned and phylogenetically characterized chickpea NFR1 and NFR5, which are showing significant homology with other legume NFR receptors. Homology modelling and molecular dynamics simulations highlight the molecular structure of ligand binding ectodomains [EDs] and cytosolic kinase domains [KDs] of NFRs in chickpea. Our detailed structural analysis also revealed that both NFR1 and NFR5 share resemblance as well as dissimilarity in sequence, structure and substrate-binding pocket. Further, molecular docking simulations provide us adequate insights into the active site of receptors where the Nod factor (NF) binds. The outcome of this work sheds light on the binding specificity of NFs towards NFRs and thus may significantly contribute to the design of new strategies in improving root-nodule symbiosis towards meeting the agricultural demands.
质膜结合受体蛋白在感知和进一步传递调节信号中起着至关重要的作用，从而调节众多发育和代谢事件。豆科植物结瘤因子受体（NFR）介导的信号的精确作用和精细调节是根瘤共生的关键要求。在这里，我们鉴定、克隆并系统发育分析了鹰嘴豆 NFR1 和 NFR5，它们与其他豆科植物 NFR 受体具有显著的同源性。同源建模和分子动力学模拟突出了鹰嘴豆 NFR 配体结合外域（ED）和胞质激酶域（KD）的分子结构。我们详细的结构分析还表明，NFR1 和 NFR5 在序列、结构和底物结合口袋上既有相似之处，也有不同之处。此外，分子对接模拟为我们提供了对受体活性位点的深入了解，其中 Nod 因子（NF）结合在该位点。这项工作的结果阐明了 NF 对 NFR 的结合特异性，因此可能对设计新策略以提高根瘤共生以满足农业需求有重要贡献。
