FUNCTIONAL-SIGNIFICANCE OF FLEXIBILITY IN PROTEINS
FUNCTIONAL-SIGNIFICANCE OF FLEXIBILITY IN PROTEINS
复制标题
DOI：
10.1002/bip.360220136
复制
发表时间：
1983-01-01
期刊：
影响因子：
2.9
通讯作者：
BENNETT, WS
中科院分区：
文献类型：
--
作者：
HUBER, R;BENNETT, WS
对三个系统：胰酶-胰酶原、免疫球蛋白和柠檬酸合成酶，讨论了大规模柔性的结构基础和功能含义。胰酶-胰酶原系统提供了一个例子，其中有序-无序转变被用作调节酶活性的一种手段。免疫球蛋白展示了如何使用灵活连接的结构域来允许具有不同排列的配体结合。在柠檬酸合成酶中，结构域运动形成一个不受溶剂影响的活性部位。在其他一些系统中也观察到了类似的大规模灵活性。
The structural basis and the functional implications of large‐scale flexibility are discussed for three systems: trypsin–trypsinogen, immunoglobulins, and citrate synthase. The trypsin–trypsinogen system provides an example in which an order–disorder transition is used as a means to regulate enzymatic activity. Immunoglobulins demonstrate how flexibly linked domains may be used to allow the binding of ligands with diverse arrangements. In citrate synthase, domain motion forms an active site that is shielded from solvent. Analogous large‐scale flexibility has been observed in a number of other systems.