The glycophorin A transmembrane domain dimer: sequence-specific propensity for a right-handed supercoil of helices.
The glycophorin A transmembrane domain dimer: sequence-specific propensity for a right-handed supercoil of helices.
复制标题
DOI：
10.1021/bi00166a003
复制
发表时间：
1992-12
期刊：
影响因子：
2.9
通讯作者：
H. Treutlein;M. Lemmon;D. Engelman;A. Brunger
中科院分区：
文献类型：
--
作者：
H. Treutlein;M. Lemmon;D. Engelman;A. Brunger
最近的研究表明，跨膜螺旋协会在一系列功能的具体作用，但这些相互作用的构象和能量学的理解一直难以捉摸。我们已经研究了特异性二聚化的血型糖蛋白A的跨膜螺旋通过计算最小化的相互作用能的大量的构象，使用模拟退火技术和测试的突变分析数据的模型。我们发现，二聚体是最好的建模为一个右手的超螺旋与广泛的区域紧密包装沿着二聚体接口。此外，我们观察到一个右手的超螺旋形成的序列特异性的倾向时，从一个二聚体的螺旋与平行轴的模拟退火建模，在与转录因子GCN 4的二聚化区域相比，它显示出更普遍的左手超螺旋的高倾向。
Recent studies suggest specific roles for transmembrane helix association in a range of functions, but understanding of the conformation and energetics of these interactions has been elusive. We have studied the specific dimerization of the transmembrane helix of glycophorin A by calculating the minimized interaction energies of a large number of conformations using simulated annealing techniques and tested the models against mutational analysis data. We find that the dimer is best modeled as a right-handed supercoil with an extensive region of close packing along the dimer interface. Furthermore, we observe a sequence-specific propensity for a right-handed supercoil to form when starting the simulated annealing modeling from a dimer of helices with parallel axes, in contrast with the dimerization region of the transcription factor GCN4 which shows a high propensity for the more prevalent left-handed supercoiling.