Su M W, Benson-Chanda V, Vissing H, Ramirez F
Department of Microbiology and Immunology, Morse Institute of Molecular Genetics, State University of New York Health Science Center, Brooklyn 11203.
Genomics. 1989 Apr;4(3):438-41. doi: 10.1016/0888-7543(89)90353-4.
The organization of the exons coding for the N-terminal portion of human type II procollagen has been determined. Aside from inferring the previously unknown primary structure of type II N-propeptide, this study has revealed that this coding domain of the gene exhibits an organization uniquely distinct from those of type I and type III collagens. This finding substantiates the notion that the N-propeptide coding domains of the fibrillar collagen genes evolved under less stringent selection than those encoding the C-propeptide and triple helical regions.
已确定编码人II型原胶原N端部分的外显子的组织方式。除了推断出II型N-前肽先前未知的一级结构外，本研究还表明，该基因的这一编码结构域呈现出一种与I型和III型胶原独特不同的组织方式。这一发现证实了以下观点，即纤维状胶原基因的N-前肽编码结构域在比编码C-前肽和三螺旋区域的结构域更宽松的选择下进化。
