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首页> 外文期刊>Journal of Biomolecular Structure and Dynamics >Homology models of the tetramerization domain of six eukaryotic voltage-gated potassium channels Kv1.1-Kv1.6.
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Homology models of the tetramerization domain of six eukaryotic voltage-gated potassium channels Kv1.1-Kv1.6.

机译：六个真核电压门控钾通道Kv1.1-Kv1.6的四聚化域的同源性模型。

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摘要

The homology models of the tetramerization (T1) domain of six eukaryotic potassium channels, Kv1.1-Kv1.6, were constructed based on the crystal structure of the Shaker T1 domain. The results of amino acid sequence alignment indicate that the T1 domains of these K+ channels are highly conserved, with the similarities varying from 77% between Shaker and Kv1.6 to 93% between Kv1.2 and Kv1.3. The homology models reveal that the T1 domains of these Kv channels exhibit similar folds as those of Shaker K+ channel. These models also show that each T1 monomer consists of three distinct layers, with N-terminal layer 1 and C-terminal layer 3 facing the cytoplasm and the membrane, respectively. Layer 2 exhibits the highest structural conservation because it is located around the central hydrophobic core. For each Kv channel, four identical subunits assemble into the homotetramer architecture around a four-fold axis through the hydrogen bonds and salt bridges formed by 15 highly conserved polar residues. The narrowest opening of the pore is formed by the four conserved residues corresponding to R115 of the Shaker T1 domain. The homology models of these Kv T1 domains provide particularly attractive targets for further structure-based studies.
机译：基于摇床T1域的晶体结构，构建了六个真核钾通道Kv1.1-Kv1.6的四聚体（T1）域的同源性模型。氨基酸序列比对的结果表明，这些K +通道的T1结构域是高度保守的，相似性在Shaker和Kv1.6之间为77％，在Kv1.2和Kv1.3之间为93％。同源性模型显示这些Kv通道的T1结构域显示出与Shaker K +通道相似的折叠。这些模型还表明，每个T1单体均由三个不同的层组成，其中N端层1和C端层3分别面向细胞质和膜。第2层显示最高的结构保守性，因为它位于中心疏水核周围。对于每个Kv通道，四个相同的亚基通过氢键和由15个高度保守的极性残基形成的盐桥，围绕四倍轴组装成四聚体结构。孔的最窄开口由对应于Shaker T1域R115的四个保守残基形成。这些Kv T1域的同源性模型为进一步的基于结构的研究提供了特别有吸引力的靶标。

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