Computational analysis on non-synonymous single nucleotide polymorphisms (nsSNPs) in L-type lectin receptor kinases (LECRK) protein in Arabidopsis Thaliana

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.

L型凝集素受体激酶（L-type lectin receptor kinases, LECRK）在植物应对环境刺激的生物与非生物胁迫响应过程中发挥关键作用。在模式植物拟南芥中，目前已鉴定出45个LECRK家族成员，但其具体功能仍未完全阐明。本研究针对与L型凝集素蛋白相关的单核苷酸多态性（single nucleotide polymorphism, SNPs）及其突变对该蛋白结构与功能的影响开展了全面分析，采用的计算工具涵盖了针对候选SNPs的序列与结构两类分析方法。进化分析鉴定出了保守氨基酸残基：其中处于埋藏状态的残基对蛋白结构至关重要，而暴露于表面的残基则与功能密切相关，上述两类残基的突变均可能影响蛋白的胁迫响应能力。本研究筛选出多个具有显著影响的突变位点，包括M411I、S415C、W431C、A442S、L445F、Q389K、H458Y及E651V，上述突变均可能破坏蛋白的结构或功能。其中，分子对接研究显示S415C与W431C这两个突变体的影响最为显著，极有可能破坏蛋白-蛋白相互作用。分子动力学模拟与主成分分析进一步验证了高风险突变所引发的蛋白结构与功能变化。