Babu Y S, Sack J S, Greenhough T J, Bugg C E, Means A R, Cook W J
Nature. 1985;315(6014):37-40. doi: 10.1038/315037a0.
The three-dimensional structure of calmodulin has been determined crystallographically at 3.0 A resolution. The molecule consists of two globular lobes connected by a long exposed alpha-helix. Each lobe binds two calcium ions through helix-loop-helix domains similar to those of other calcium-binding proteins. The long helix between the lobes may be involved in interactions of calmodulin with drugs and various proteins.
钙调蛋白的三维结构已通过晶体学方法以3.0埃的分辨率确定。该分子由两个球状叶组成,通过一个长的暴露α螺旋相连。每个叶通过类似于其他钙结合蛋白的螺旋-环-螺旋结构域结合两个钙离子。叶之间的长螺旋可能参与钙调蛋白与药物及各种蛋白质的相互作用。