Bocharov E V, Gudkov A T, Budovskaya E V, Arseniev A S
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow.
FEBS Lett. 1998 Feb 27;423(3):347-50. doi: 10.1016/s0014-5793(98)00121-5.
Isolated N- (1-37) and C-terminal (47-120) fragments of L7 protein, and pentameric (L7)4L10 complex were studied by NMR spectroscopy in solution. The results indicate that the dimer state of the 1-37 fragment with a helical hairpin conformation is identical to the N-terminal structure of the intact L7 dimer. The C-terminal domain of the L7 protein does not participate in (L7)4L10 complex formation. The overall motions of the L7 C-domains are essentially independent both in the L7 dimer and in the (L7)4L10 complex. Conformational motions on a millisecond time scale are detected in the (L7)4L10 complex. The possible relevance of these motions to the biological function of L7/L12 is discussed.
通过溶液核磁共振光谱研究了L7蛋白的分离N端（1-37）和C端（47-120）片段以及五聚体（L7）4L10复合物。结果表明，具有螺旋发夹构象的1-37片段的二聚体状态与完整L7二聚体的N端结构相同。L7蛋白的C端结构域不参与（L7）4L10复合物的形成。L7 C结构域在L7二聚体和（L7）4L10复合物中的整体运动基本独立。在（L7）4L10复合物中检测到毫秒时间尺度上的构象运动。讨论了这些运动与L7/L12生物学功能的可能相关性。
