CAJ | 학술논문

蛋白酪氨酸磷酸酯酶1B(PTP1B)在胰岛素受体去磷酸化过程中发挥重要作用.本研究目的在于阐述PTP1B催化位点中Arg 221的作用.各种Arg 221的突变体通过HyperChem Release 7.0软件生成.结果表明Arg 221的突变会对底物与蛋白相互作用产生显著影响.当Arg 221突变为碱性残基时,底物与蛋白之间总静电相互作用能增加,但与催化相关残基的静电相互作用能降低,其余的突变则导致底物与蛋白之间总静电相互作用能降低.这一结果表明,Arg 221突变为碱性残基町减弱PTP1B的催化活性,但使底物与蛋白的结合能力增强,其余的突变则会同时减弱酶的催化活性及底物与蛋白的结合能力.
단백락안산린산지매1B(PTP1B)재이도소수체거린산화과정중발휘중요작용.본연구목적재우천술PTP1B최화위점중Arg 221적작용.각충Arg 221적돌변체통과HyperChem Release 7.0연건생성.결과표명Arg 221적돌변회대저물여단백상호작용산생현저영향.당Arg 221돌변위감성잔기시,저물여단백지간총정전상호작용능증가,단여최화상관잔기적정전상호작용능강저,기여적돌변칙도치저물여단백지간총정전상호작용능강저.저일결과표명,Arg 221돌변위감성잔기정감약PTP1B적최화활성,단사저물여단백적결합능력증강,기여적돌변칙회동시감약매적최화활성급저물여단백적결합능력.
Protein tyrosine phosphatase 1B (PTP1B) plays a major role in regulation of dephosphorylation of insulin receptor. The present study was designed to elucidate the effect of Arg 221 in catalytic site. Mutants of Arg 221 were carried out using the computer program HyperChem Release 7.0. The variation of Arg 221 had significant effects on the interaction of substrate with protein. When Arg 221 mutated to basic residues, the electrostatic interaction energies between substrate and protein increased but the contribution of catalytic residues decreased. Other mutations caused decrease in total electrostatic interaction energies. Our data suggested that mutations of Arg 221 to basic residues decreased the catalytic activity but increased the binding affinity for substrate, and mutations to others would decrease both catalytic and binding abilities.