Pl(4,5)P2 contains two long-chain fatty acids that play the role of promoting micelle formation. Cellular form of Pl(4,5)P2 also contains stearate at position 1 and arachidonate at position 2 of glycerol group. Substoichiometric addition of amounts of Pl(4,5)P2 species in myristoylated MA and myristoylated MA lead to stern broadening in the 1H-14N (HSQC) NMR spectra. It also led to the signals for NH groups to broaden beyond detection (Bhardwaj, 56).

Myristyl is very crucial in the replication process of Late phase HIV type 1, however, the mutation process can hamper with myristoylation process leading to inhibition of membrane binding in vitro. This can result in Gag targeting cytoplasm and other intercellular membranes instead of the plasma membrane. Occasionally, Gag molecules are known to assemble and bud from the plasma membrane via indirect routing (Bhardwaj, 81). On the other hand, in primary macrophages budding was found to be occurring in multivesicular bodies.

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According to the research carried out, localization of Gag molecules in virus assembly depends on Pl(4,5)Pz. Pl(4,5)Pz also plays a significant role in marking membranes of specific cellular proteins. Depletion of Pl(4,5)Pz hampers virus assembly and results in piling of Gag molecules at membranes of late endosomes and MVBs (21). On the other hand, induction of Pl(4,5)Pz filled with endosomes redirects Gag into targeting endosomes or MVBs. Induction also stimulates intravesical budding. The replacement of MA with membrane-binding N end Fyn kinase results in a reduction of virus sensitivity in assembling to Pl(4,5)P2 that results in manipulation.

In the study of the structure of di-C4-Pl(4,5)P2:myrMA Complex, it was observed that myrMA was absent. The binding of di-c4-Pl(4,5)P2 was found to be because of the elimination of the myristyl group. Exposure of myristate was found to be induced by an allosteric mechanism. This was shown by the binding that took place between di-c4-Pl(4,5)P2 and myrMA (Bhardwaj, 77). The binding of di-c4-Pl(4,5)P2 and myrMA resulted in structural changes of more. From the structural changes observed on myrMA, it was deduced that myristate exposure was triggered by an allosteric mechanism. In the process, Pl(4,5)P2 binding stimulates slight significant changes in the beta-hairpin that is responsible for the observant changes in the orientation of the helical structure.