McLaughlin S H, Bulleid N J
University of Manchester, School of Biological Sciences, UK.
Matrix Biol. 1998 Feb;16(7):369-77. doi: 10.1016/s0945-053x(98)90010-5.
Recent advances in the understanding of the molecular recognition events occurring during the assembly of procollagen during biosynthesis have come from the use of a semi-permeabilized cell-system that reconstitutes the initial steps of chain assembly as they would occur in the endoplasmic reticulum of an intact cell. This has enabled a number of key questions concerning the molecular determinants of procollagen assembly to be addressed. In particular, the recognition events underlying the initial association of individual procollagen chains have been investigated, resulting in the identification of the key residues involved within the C-propeptide of fibrillar collagens. Similarly, the role of inter-chain disulfide bond formation in chain recognition and assembly has been investigated, along with the role of the C-propeptide, C-telopeptide and proline hydroxylation in helix nucleation, alignment and propagation. The results from these studies point to a two-stage recognition event, i.e., association of the chains driven by residues within the C-propeptide followed by nucleation and alignment of the helix driven mainly by sequences present at the C-terminal end of the triple helical domain.
近年来，在理解生物合成过程中前胶原组装期间发生的分子识别事件方面取得了进展，这得益于使用了一种半透性细胞系统，该系统重构了链组装的初始步骤，就如同它们在完整细胞的内质网中发生的那样。这使得一些关于前胶原组装分子决定因素的关键问题得以解决。特别是，已经研究了单个前胶原链初始缔合背后的识别事件，从而确定了纤维状胶原C-前肽中涉及的关键残基。同样，也研究了链间二硫键形成在链识别和组装中的作用，以及C-前肽、C-端肽和脯氨酸羟基化在螺旋成核、排列和延伸中的作用。这些研究结果表明存在一个两阶段的识别事件，即由C-前肽内的残基驱动链的缔合，随后主要由三螺旋结构域C末端存在的序列驱动螺旋的成核和排列。
