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Abstract
L-type lectin receptor kinases (LECRK) plays a significant role in biotic and abiotic stress response against environmental stimuli in plants. In the Arabidopsis model plant, a total of 45 LECRK was identified but function elucidation is still unresolved. This study carried out a comprehensive analysis of the SNPs associated with L-type lectin protein and how these mutations affect the structure and function of the protein. The computational tools utilized covers both sequence and structure based analysis of the candidate SNPs. The evolutionary analysis identified the conserved residues that are either buried and structurally important or exposed means functionally important hence, can affect the stress response of the protein. A few of the significant mutations are identified M411I, S415C, W431C, A442S, L445F, Q389K, H458Y, and E651V are expected to damage the structure or function of the protein. Among them, the docking studies identified the mutants S415C and W431C as most crucial which can most likely disrupt the protein-protein interactions. Molecular dynamic simulation and principal component analysis further highlights the structural and functional changes in protein resulting by high risks mutations.
Published Version
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