通过定点诱变抑制核心蛋白聚糖结构域I的糖胺聚糖修饰会改变蛋白酶敏感性和层粘连蛋白-1结合活性。
Inhibition of glycosaminoglycan modification of perlecan domain I by site-directed mutagenesis changes protease sensitivity and laminin-1 binding activity.
作者信息
Sasaki T, Costell M, Mann K, Timpl R
机构信息
Max-Planck-Institut für Biochemie, Martinsried, Germany.
出版信息
FEBS Lett. 1998 Sep 18;435(2-3):169-72. doi: 10.1016/s0014-5793(98)01063-1.
PMID:9762901
Abstract
Glycosaminoglycan attachment to perlecan domain I (173 residues) was completely prevented by site-directed mutagenesis of Ser-65, Ser-71 and Ser-76 as shown by recombinant production in mammalian cells. This did not interfere with the proper folding of the domain's SEA module but enhanced its sensitivity to neutral proteases. Lack of substitution also abolished binding to the two major heparin binding sites of laminin-1.
摘要
如在哺乳动物细胞中的重组生产所示，通过对丝氨酸-65、丝氨酸-71和丝氨酸-76进行定点诱变，可完全阻止糖胺聚糖附着于核心蛋白聚糖结构域I（173个残基）。这并不干扰该结构域SEA模块的正确折叠，但增强了其对中性蛋白酶的敏感性。缺乏取代作用也消除了与层粘连蛋白-1的两个主要肝素结合位点的结合。
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