Crystal Structures of BMH: CaM-M13 and 83-84Calmodulin

钙调蛋白是信使钙的主要换能器。它被认为存在于所有真核生物的所有细胞的细胞质中。它以钙的形式（而不是其他形式）激活了至少10种，甚至可能多达20种不同的酶或结构蛋白。它是通过基因复制进化而来的，尤其在动物中是高度保守的。先前的晶体结构研究表明，钙调蛋白由两个由短肽连接链连接的蛋白裂片组成。本课题拟研究钙调蛋白相关蛋白的两种晶体结构。适合x射线衍射研究的晶体已经生长出来了。这些决定的意义在于他们对模型的测试，在模型中，钙调蛋白的中心连接器作为一种灵活的系绳起作用，允许两个标签上的特定补丁包裹靶标。

The protein calmodulin is the principle transducer of messenger calcium. It is believed to exist within the cytosols of all cells of all eukaryotes. In its calcium forms, (but not in other forms) it activates at least ten and probably as many as twenty different enzymes or structural proteins. It has evolved by gene duplication and is very highly conserved especially among the animals. Previous crystal structure studies have revealed that calmodulin consists of two protein lobes joined by a short pepitde linking chain. This proposal is to study two crystal structures of proteins related to calmodulin. Crystals suitable for x-ray diffraction studies have already been grown. The significance of these determinations is their test of the model in which the central linker of calmodulin functions as a flexible tether allowing specific patches on the two labels to enfold a target.