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首页> 外文期刊>Journal of Molecular Biology >Site-specific structural variations accompanying tubular assembly of the hiv-1 capsid protein
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Site-specific structural variations accompanying tubular assembly of the hiv-1 capsid protein

机译：hiv-1衣壳蛋白的管状组装伴随的位点特异性结构变异

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摘要

The 231-residue capsid (CA) protein of human immunodeficiency virus type 1 (HIV-1) spontaneously self-assembles into tubes with a hexagonal lattice that is believed to mimic the surface lattice of conical capsid cores within intact virions. We report the results of solid-state nuclear magnetic resonance (NMR) measurements on HIV-1 CA tubes that provide new information regarding changes in molecular structure that accompany CA self-assembly, local dynamics within CA tubes, and possible mechanisms for the generation of lattice curvature. This information is contained in site-specific assignments of signals in two- and three-dimensional solid-state NMR spectra, conformation-dependent 15N and 13C NMR chemical shifts, detection of highly dynamic residues under solution NMR conditions, measurements of local variations in transverse spin relaxation rates of amide 1H nuclei, and quantitative measurements of site-specific 15N-15N dipole-dipole couplings. Our data show that most of the CA sequence is conformationally ordered and relatively rigid in tubular assemblies and that structures of the N-terminal domain (NTD) and the C-terminal domain (CTD) observed in solution are largely retained. However, specific segments, including the N-terminal β-hairpin, the cyclophilin A binding loop, the inter-domain linker, segments involved in intermolecular NTD-CTD interactions, and the C-terminal tail, have substantial static or dynamical disorder in tubular assemblies. Other segments, including the 310-helical segment in CTD, undergo clear conformational changes. Structural variations associated with curvature of the CA lattice appear to be localized in the inter-domain linker and intermolecular NTD-CTD interface, while structural variations within NTD hexamers, around local 3-fold symmetry axes, and in CTD-CTD dimerization interfaces are less significant.
机译：1型人类免疫缺陷病毒（HIV-1）的231个残基衣壳（CA）蛋白自发自组装成带有六边形格子的管，该六边形格子被认为可模仿完整病毒体中圆锥形衣壳核心的表面格子。我们报告了对HIV-1 CA管的固态核磁共振（NMR）测量的结果，这些结果提供了有关伴随CA自组装，CA管内局部动力学以及产生CA的可能机理的分子结构变化的新信息。晶格曲率。此信息包含在二维和三维固态NMR光谱中信号的特定位置分配中，依赖构象的15N和13C NMR化学位移，在溶液NMR条件下检测高动态残留物，测量横向的局部变化酰胺1H核的自旋弛豫速率，以及定点15N-15N偶极-偶极偶合的定量测量。我们的数据表明，大多数CA序列在管状装配中呈构象有序且相对刚性，并且在溶液中观察到的N末端结构域（NTD）和C末端结构域（CTD）的结构得以保留。但是，包括N末端β-发夹，亲环蛋白A结合环，域间连接子，分子间NTD-CTD相互作用所涉及的片段以及C​​末端尾部的特定片段在肾小管中具有明显的静态或动态障碍组件。其他节段，包括CTD中的310螺旋节段，均发生明显的构象变化。与CA晶格的曲率相关的结构变化似乎位于域间连接子和分子间NTD-CTD界面中，而NTD六聚体，局部3倍对称轴周围以及CTD-CTD二聚化界面中的结构变化较小重大。

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