When a predicted coiled coil is really a single α-helix, in myosins and other proteins
When a predicted coiled coil is really a single α-helix, in myosins and other proteins
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DOI：
10.1039/b822339d
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发表时间：
2009-01-01
期刊：
影响因子：
3.4
通讯作者：
Knight, Peter J.
中科院分区：
文献类型：
--
作者：
Peckham, Michelle;Knight, Peter J.
裸露的单α螺旋在蛋白质中是不常见的。最近，我们发现预测的卷曲螺旋结构域的一些肌球蛋白实际上是一个稳定的单α螺旋（SAH）。因此，这些蛋白质不通过卷曲螺旋形成二聚化，如先前所假设的。由于SAH结构域很好地延长了杠杆，它可以使这些肌球蛋白采取比以前假设的更大的步骤。现在越来越清楚的是，大量不同的蛋白质都含有这个以前被忽视的结构域。SAH通常被预测软件错误地识别为卷曲螺旋结构域，并且对潜在SAH序列的初始扫描表明，人类蛋白质组中高达4%的预测具有卷曲螺旋结构域的蛋白质实际上具有SAH结构域。本文综述了近年来有关SAH结构域的研究结果，它们的性质，潜在功能以及如何识别它们的一些线索。
Naked single alpha-helices are unusual in proteins. Recently, we discovered that the predicted coiled-coil domain of some myosins was in fact a stable single alpha-helix (SAH). As a consequence these proteins do not dimerise through coiled-coil formation as previously assumed. As the SAH domain is well placed to lengthen the lever, it could enable these myosins to take larger steps than has been previously assumed. It is now becoming clear than a substantial number of diverse proteins contain this previously overlooked domain. SAHs are commonly misidentified as coiled-coil domains by prediction software and an initial scan for potential SAH sequences suggests that up to 4% of proteins in the human proteome predicted to have a coiled-coil domain actually have a SAH domain instead. This review summarises recent findings on SAH domains, their properties, their potential functions and some clues on how to recognise them.