Allosteric regulation of chaperonins
Allosteric regulation of chaperonins
复制标题
DOI：
10.1016/j.sbi.2005.10.001
复制
发表时间：
2005-12-01
影响因子：
6.8
通讯作者：
Willison, KR
中科院分区：
文献类型：
--
作者：
Horovitz, A;Willison, KR
伴侣蛋白是分子机器，其通过经历能量（ATP）依赖性运动来促进蛋白质折叠，所述运动通过复杂的变构调节在时间和空间上协调。最近，在描述这些机器的各种功能（变构）状态，它们相互转换的途径，以及变构转换和蛋白质折叠反应之间的耦合方面取得了进展。然而，各种机制问题仍有待解决。
Chaperonins are molecular machines that facilitate protein folding by undergoing energy (ATP)-dependent movements that are coordinated in time and space by complex allosteric regulation. Recently, progress has been made in describing the various functional (allosteric) states of these machines, the pathways by which they interconvert, and the coupling between allosteric transitions and protein folding reactions. However, various mechanistic issues remain to be resolved.