In Silico structural analysis of the complex PSKR receptor like Kinase, Pamp Phytosulfokine and SERk1 co-receptor

Abstract

Plants often have to undergo pathogen invasions in nature. Nevertheless, as a result of proficient immune systems owned by the host plants, plant diseases seldom occur. In the process two separate recognition mechanisms identify pathogens, and one of them is known as pattern-triggered immunity (PTI) which plays an essential role in plant defense system. PRRs preliminarily conjoin to the pathogen-associated molecular patterns (PAMPs) in the case of a microbial incursion and then go on to ever further assigned co-receptor proteins to stimulate the defensive signal and optimize the immune response of the plant. While many plant PRRs have been found, only few have been thoroughly described and their structural specifications have been analyzed. In this analysis, the PSKR-Phytosulfokine-SERk1 (PDB ID: 4z64) complex crystallographic structure was simulated for 30 ns at several phases, as there were five different composites of the prime crystallographic composition. In order to obtain a synopsis of the interaction and immune responsiveness of PSKR against Phytosulfokine with the aid of co-receptor SERk1, 30ns of simulated trajectories were studied for each amalgamation. In addition, it was found here that from Phytosulfokine, Thr31 and Gln32 made a notable con tribution to the PSKR-Phytosulfokine complex development. It indicates that Phytosulfokine interacts predominantly with a β-strand from the PSKRR island domain and the development of an anti- β -sheet takes place in the process. Therefore, any alteration to the PAMP at these positions can be expected to be dramatically pernicious to the plant, resulting in the PRR failing its ability to detect the PAMP. As PSKR has been observed to play a key role in the plant defense mechanism of Arabidopsis thaliana, its theorized binding method with Phytosulfokine and SERk1 co-receptor can guide to draw a clearer picture of PTI's initial phases.