Lupas A, Van Dyke M, Stock J
Department of Molecular Biology, Princeton University, NJ 08544.
Science. 1991 May 24;252(5009):1162-4. doi: 10.1126/science.252.5009.1162.
The probability that a residue in a protein is part of a coiled-coil structure was assessed by comparison of its flanking sequences with sequences of known coiled-coil proteins. This method was used to delineate coiled-coil domains in otherwise globular proteins, such as the leucine zipper domains in transcriptional regulators, and to predict regions of discontinuity within coiled-coil structures, such as the hinge region in myosin. More than 200 proteins that probably have coiled-coil domains were identified in GenBank, including alpha- and beta-tubulins, flagellins, G protein beta subunits, some bacterial transfer RNA synthetases, and members of the heat shock protein (Hsp70) family.
通过将蛋白质中某一残基的侧翼序列与已知卷曲螺旋蛋白的序列进行比较，评估该残基成为卷曲螺旋结构一部分的概率。此方法用于在其他方面呈球状的蛋白质中描绘卷曲螺旋结构域，比如转录调节因子中的亮氨酸拉链结构域，还用于预测卷曲螺旋结构内的间断区域，比如肌球蛋白中的铰链区。在GenBank中鉴定出了200多种可能具有卷曲螺旋结构域的蛋白质，包括α-和β-微管蛋白、鞭毛蛋白、G蛋白β亚基、一些细菌转移RNA合成酶以及热休克蛋白（Hsp70）家族的成员。
