Surya Sukumaran, Abhilash Joseph, Geethanandan Krishnan, Sadasivan Chittalakkottu, Haridas Madhathilkovilakathu
Inter University Centre for Bioscience and Department of Biotechnology and Microbiology, Kannur University, Thalassery Campus, Kannur 670661, India.
Int J Biol Macromol. 2016 Jun;87:529-36. doi: 10.1016/j.ijbiomac.2016.02.081. Epub 2016 Mar 2.
Proteins may utilize complex networks of interactions to create/proceed signaling pathways of highly adaptive responses such as programmed cell death. Direct binary interactions study of proteins may help propose models for protein-protein interaction. Towards this goal we applied a combination of thermodynamic kinetics and crystal structure analyses to elucidate the complexity and diversity in such interactions. By determining the heat change on the association of two galactose-specific legume lectins from Butea monosperma (BML) and Spatholobus parviflorus (SPL) belonging to Fabaceae family helped to compute the binding equilibrium. It was extended further by X-ray structural analysis of BML-SPL binary complex. In order to chart the proteins interacting mainly through their interfaces, identification of the nature of forces which stabilized the association of the lectin-lectin complex was examined. Comprehensive analysis of the BMLSPL complex by isothermal titration calorimetry and X-ray crystal structure threw new light on the lectin-lectin interactions suggesting of their use in diverse areas of glycobiology.
蛋白质可能利用复杂的相互作用网络来创建/推进高度适应性反应的信号通路，如程序性细胞死亡。对蛋白质直接二元相互作用的研究可能有助于提出蛋白质-蛋白质相互作用的模型。为了实现这一目标，我们应用了热力学动力学和晶体结构分析相结合的方法来阐明此类相互作用中的复杂性和多样性。通过测定来自豆科植物单籽紫铆（BML）和小花血藤（SPL）的两种半乳糖特异性豆科凝集素结合时的热变化，有助于计算结合平衡。通过对BML-SPL二元复合物的X射线结构分析进一步扩展了这一研究。为了描绘主要通过其界面相互作用的蛋白质，研究了稳定凝集素-凝集素复合物结合的力的性质。通过等温滴定量热法和X射线晶体结构对BML-SPL复合物进行的综合分析，为凝集素-凝集素相互作用提供了新的线索，表明它们可用于糖生物学的不同领域。
