Chen C H, Clegg D O, Hansma H G
Department of Physics, University of California, Santa Barbara 93106, USA.
Biochemistry. 1998 Jun 2;37(22):8262-7. doi: 10.1021/bi973097j.
Laminins are a family of multifunctional extracellular matrix glycoproteins that play important roles in the development and maintenance of tissue organization via their interactions with cells and other extracellular matrix proteins. To understand the structural basis of laminins' functions, we examined the motion of laminin-1 (Ln-1) in physiological buffers using atomic force microscopy. While many Ln-1 molecules assumed the expected cruciform structure, unexpected dynamic movements of the Ln-1 arms were observed in aqueous environments. These dynamic movements of the Ln-1 arms may contribute to the diversity of laminin functions.
层粘连蛋白是一类多功能细胞外基质糖蛋白，它们通过与细胞及其他细胞外基质蛋白相互作用，在组织的发育和维持中发挥重要作用。为了理解层粘连蛋白功能的结构基础，我们使用原子力显微镜在生理缓冲液中研究了层粘连蛋白-1（Ln-1）的运动。虽然许多Ln-1分子呈现出预期的十字形结构，但在水性环境中观察到Ln-1臂出现了意外的动态运动。Ln-1臂的这些动态运动可能有助于层粘连蛋白功能的多样性。
