Folding and regulation in myosins II and V.
Folding and regulation in myosins II and V.
复制标题
肌球蛋白 II 和 V 的折叠和调节。
DOI：
10.1007/s10974-008-9134-0
复制
发表时间：
2007
影响因子：
2.7
通讯作者：
Knight,PeterJ
中科院分区：
文献类型：
--
作者：
Sellers,JamesR;Knight,PeterJ
The enzymatic activity of many myosins is regulated by various means including calcium binding, phosphorylation or binding of receptor molecules. In this review we compare and contrast the regulation of smooth muscle myosin II and myosin Va with particular emphasis on the structural basis for the regulation. Both myosins adopt folded compact conformations in their off states, but the details of the conformations are markedly different. In the regulated smooth muscle myosin II, the key feature is an asymmetric interaction between the two heads of the molecule with contributions of specific tail–head interactions. In myosin V the key feature is an interaction between the heads and the globular tail domain.
