Reid R E
J Theor Biol. 1985 Jun 7;114(3):353-74. doi: 10.1016/s0022-5193(85)80171-5.
Examination of the interaction of major tranquilizers with calmodulin results in the generalization that the functional nature of calcium binding helix-loop-helix regions found in several calcium binding proteins including calmodulin, troponin C and parvalbumin is dependent upon the topography of the hydrophobic and hydrophilic regions on the amphiphilic N-terminal alpha-helix of the helix-loop-helix conformation formed by the binding of the calcium cation to these proteins. The relation of the topography of this amphiphilic alpha-helix to drug binding is delineated at the molecular level and the results obtained are used to describe the interaction of beta-endorphin, dynorphin, alpha-MSH and other peptides with calmodulin. The utility of this hypothesis is further demonstrated by the description of a possible interaction between troponin C, troponin I and troponin T of the troponin complex in skeletal muscle.
在包括钙调蛋白、肌钙蛋白C和小清蛋白在内的几种钙结合蛋白中发现的钙结合螺旋-环-螺旋区域的功能性质，取决于钙阳离子与这些蛋白结合形成的螺旋-环-螺旋构象的两亲性N端α-螺旋上疏水和亲水区域的拓扑结构。在分子水平上描绘了这种两亲性α-螺旋的拓扑结构与药物结合的关系，并将所得结果用于描述β-内啡肽、强啡肽、α-促黑素细胞激素和其他肽与钙调蛋白的相互作用。通过描述骨骼肌中肌钙蛋白复合物的肌钙蛋白C、肌钙蛋白I和肌钙蛋白T之间可能的相互作用，进一步证明了这一假设的实用性。
