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首页> 外文期刊>Journal of Molecular Biology >Structural analysis of the N-terminal domain of the human T-cell leukemiavirus capsid protein
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Structural analysis of the N-terminal domain of the human T-cell leukemiavirus capsid protein

机译：人T细胞白血病病毒衣壳蛋白N末端结构域的结构分析

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The N-terminal domain of the retroviral capsid (CA) protein is one of the least conserved regions encoded in the genome. Surprisingly, the three-dimensional structures of the CA from different genera exhibit alpha -helical structural features that are highly conserved. The N-terminal residues of the human immunodeficiency virus type 1 (HIV-1) and Rous sarcoma virus (RSV) capsid proteins form a beta -hairpin. To determine if this feature is conserved in the retroviral family, we cloned, expressed, purified, and solved the structure of a N-terminal 134 amino acid fragment (CA(134)) from the human T-cell leukemia virus type 1 (HTLV-I) using high resolution nuclear magnetic resonance (NMR) spectroscopy. The CA(134) fragment contains an N-terminal beta -hairpin and a central coiled-coil-like structure composed of six alpha -helices. The N-terminal Pro1 residue contacts Asp54 in the helical cluster through a salt bridge. Thus, the beta -hairpin is conserved and the helical cluster is structurally similar to other retroviral CA domains. However, although the same Asp residue defines the orientation of the hairpin in both the HTLV-1 and HIV-1 CA proteins, the HTLV-I hairpin is oriented away, rather than towards, the helical core. Significant differences were also detected in the spatial orientation and helical content of the long centrally located loop connecting the helices in the core. It has been proposed that the salt bridge allows the formation of a CA-CA interface that is important for the assembly of the conical cores that are characteristic of HIV-1. As HTLV-I forms spherical cores, the salt-bridge feature is apparently not conserved for this function although its role in determining the orientation of the beta -hairpin may be critical, along with the central loop. Comparison of three-dimensional structures is expected to elucidate the relationships between the retroviral capsid protein structure and its function.
机译：逆转录病毒衣壳（CA）蛋白的N末端域是基因组中编码的最不保守的区域之一。令人惊讶地，来自不同属的CA的三维结构表现出高度保守的α-螺旋结构特征。 1型人类免疫缺陷病毒（HIV-1）和劳斯肉瘤病毒（RSV）衣壳蛋白的N末端残基形成一个β-发夹结构。为了确定该功能在逆转录病毒家族中是否保守，我们克隆，表达，纯化并解决了人类T细胞白血病病毒1型（HTLV）N端134个氨基酸片段（CA（134））的结构-I）使用高分辨率核磁共振（NMR）光谱。 CA（134）片段包含一个N端β-发夹和一个由六个α-螺旋组成的中央螺旋状线圈结构。 N末端Pro1残基通过盐桥与螺旋簇中的Asp54接触。因此，β-发夹是保守的，并且螺旋簇在结构上类似于其他逆转录病毒CA结构域。但是，尽管相同的Asp残基定义了HTLV-1和HIV-1 CA蛋白中发夹的方向，但是HTLV-1发夹的方向是远离螺旋核心，而不是朝向螺旋核心。还发现了连接核心中螺旋的位于中心的长环的空间方向和螺旋含量的显着差异。已经提出，盐桥允许形成CA-CA界面，这对于组装具有HIV-1特征的圆锥形核是重要的。当HTLV-1形成球形核时，盐桥特征显然不适合该功能，尽管其在确定β-发夹的方向中的作用以及中心环可能至关重要。三维结构的比较有望阐明逆转录病毒衣壳蛋白结构与其功能之间的关系。

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