为从变形体 berghei 的氮的氧化物 synthase 和类似的蛋白质的结构和功能的生物信息学分析和预言

摘要

正Objective:To search and analyze nitric oxide synthase(NOS) and similar proteins from Plasmodium berghei(Pb).Methods:The structure and function of nitric oxide synthase and similar proteins from Plasmodium berghei were analyzed and predicted by bioinformatics. Results:P6NOS were not available,but nicotinamide adenine dinucleotide 2’-phosphate reduced tetrasodium(NADPH)-cytochrome p450 reductase(CPR) were gained.PiCPR was in the nucleus of Plasmodium berghei,while 134aa-229aa domain was localize in nucleolar organizer. The amino acids sequence of P6CPR had the closest genetic relationship with Plasmodium vivax showing a 73%homology.The tertiary structure of PbCPR displayed the forcep-shape with wings,but no wings existed in the tertiary structure of its’ host,Mus musculus(Mm).137aa-200aa, 201aa-218aa,220aa-230aa,232aa-248,269aa-323aa,478aa-501aa and 592aa-606aa domains of P6CPR showed no homology with MmCPRs’,and all domains were exposed on the surface of the protein.Conclusions:NOS can’t be found in Plasmodium berghei and other Plasmodium species.PbCPR may be a possible resistance site of antimalarial drug,and the targets of antimalarial drug and vaccine.It may be also one of the mechanisms of immune evasion.This study on Plasmodium berghei may be more suitable to Plasmodium vivax.And137aa-200aa, 201aa-218aa,220aa-230aa,232aa-248,269aa-323aa,478aa-501aa and 592aa-606aa domains of PbCPR are more ideal targets of antimalarial drug and vaccine.