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首页> 外文期刊>RSC Advances >Role of tryptophan 135 of Chandipura virus phosphoprotein P in dimerization and complex formation with leader RNA: structural aspect using time resolved anisotropy and simulation
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Role of tryptophan 135 of Chandipura virus phosphoprotein P in dimerization and complex formation with leader RNA: structural aspect using time resolved anisotropy and simulation

机译：Chandipura病毒磷蛋白P色氨酸135在二聚化和前导RNA形成复合物中的作用：使用时间分辨各向异性和模拟的结构方面

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摘要

The aggregation of phosphoprotein P of Chandipura virus (CHPV) and its interaction with viral leader (le) RNA in aqueous buffer and 40% ethylene glycol (EG)-buffer have been characterised using two single tryptophan (Trp/W) mutants W105F and W135F. The longer rotational correlation time [(theta(C))(T)] originating from overall motion observed at 300 nM concentration conforms to a globular structure of the monomer of WT and both the mutants. The (theta(C))(T) values also indicate that W135F does not form a dimer at 1500 nM concentration; while a dimer with disordered structure is predicted for both WT and W105F. The complexes of WT and W105F with le RNA at monomeric and dimeric conditions are indicated to have tight core packing. Dimerization and complex formation at both the concentrations enhance the correlation time arising from the localised motion of Trp side chain [(theta(C))(S)] for WT and W105F predicting hindered localized rotation of Trp 135. Comparative protein modelling and molecular dynamics (MD) simulations using the amino acids domain ranging from 105-168 of the full length CHPVP based on the vesicular stomatitis virus phosphoprotein (VSVP) also indicate that formation of dimers are more feasible for WT and W105F compared to W135F.
机译：使用两个单个色氨酸（Trp / W）突变体W105F和W135F表征了Chandipura病毒（CHPV）的磷蛋白P的聚集及其在水性缓冲液和40％乙二醇（EG）缓冲液中与病毒前导（le）RNA的相互作用。源自300nM浓度下的整体运动的较长旋转相关时间[（theta（C））（T）]与WT单体和两个突变体的球形结构一致。 （theta（C））（T）值还表明W135F在1500 nM浓度下不会形成二聚体。 WT和W105F均可预测结构紊乱的二聚体。 WT和W105F与le RNA在单体和二聚体条件下的复合物表明具有紧密的核堆积。两种浓度下的二聚化和复合物形成均增加了WT和W105F的Trp侧链[（theta（C））（S）]的局部运动所产生的相关时间，从而预测了Trp 135的受阻局部旋转。比较蛋白质建模和分子动力学（MD）使用基于水泡性口炎病毒磷蛋白（VSVP）的全长CHPVP的105-168氨基酸结构域进行的模拟（MD）也表明，与W135F相比，WT和W105F的二聚体形成更为可行。

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