印度单环眼镜蛇（眼镜王蛇）的NK-CT1分子建模及其与人DNA拓扑异构酶IIα的对接相互作用。
Molecular modeling of NK-CT1, from Indian monocellate cobra (Naja kaouthia) and its docking interaction with human DNA topoisomerase II alpha.
作者信息
Bandopadhyay Pathikrit, Halder Soma, Sarkar Mrinmoy, Kumar Bhunia Sujay, Dey Sananda, Gomes Antony, Giri Biplab
机构信息
Experimental Medicine and Stem Cell Research Laboratory, Department of Physiology, West Bengal State University, Barasat, Kolkata 700 126, West bengal, India; University of Kalyani, Kalyani 741 235, West Bengal, India.
Experimental Medicine and Stem Cell Research Laboratory, Department of Physiology, West Bengal State University, Barasat, Kolkata 700 126, West bengal, India.
出版信息
Bioinformation. 2016 Jun 15;12(3):105-111. doi: 10.6026/97320630012105. eCollection 2016.
A 6.76 kDa molecular weight cardio and cytotoxic protein of 60 amino acids in length called NK-CT1, was purified from the venom of Indian monocellate cobra (Naja kaouthia) by ion-exchange chromatography and HPLC as described in our earlier report. Therefore it is of interest to utlize the sequence of NK-CT1 for further functional inference using molecular modeling and docking. Thus homology model of NK-CT1 is described in this report. The anti-proliferative activity of the protein, binding with human DNA topoisomerase-II alpha was demonstrated using docking data with AUTODOCK and AUTODOCK MGL tools. Data shows that M26, V27 and S28 of NK-CT1 is in close contact with the nucleotides of the oligonucleotide, bound with topoisomerase-II alpha complex.
一种分子量为6.76 kDa、长度为60个氨基酸的心脏毒性蛋白NK-CT1，如我们之前的报告所述，通过离子交换色谱法和高效液相色谱法从印度单型眼镜蛇（眼镜王蛇）的毒液中纯化得到。因此，利用NK-CT1的序列通过分子建模和对接进行进一步的功能推断具有重要意义。本报告描述了NK-CT1的同源模型。使用AUTODOCK和AUTODOCK MGL工具的对接数据证明了该蛋白与人类DNA拓扑异构酶-IIα结合的抗增殖活性。数据显示，NK-CT1的M26、V27和S28与与拓扑异构酶-IIα复合物结合的寡核苷酸的核苷酸紧密接触。
Zotero 插件