Tauris J, Ellgaard L, Jacobsen C, Nielsen M S, Madsen P, Thøgersen H C, Gliemann J, Petersen C M, Moestrup S K
Department of Medical Biochemistry, University of Aarhus, Denmark.
FEBS Lett. 1998 Jun 5;429(1):27-30. doi: 10.1016/s0014-5793(98)00559-6.
Binding of the receptor-associated protein (RAP) to the newly identified putative sorting receptor, sortilin, was analyzed by surface plasmon resonance analysis of recombinant RAP and sortilin domains and compared with binding to megalin and low density lipoprotein receptor-related protein (LRP). The data show that the RAP-binding site in sortilin is localized in the cysteine-rich lumenal part homologous to yeast vacuolar protein-sorting 10 protein (Vps10p), and the sortilin-binding site in RAP is localized in the carboxy-terminal domain III of the three homologous domains in RAP. Whereas sortilin bound only RAP domain III, megalin and LRP bound all RAP domains with the functional affinity order: domain III >domain I > domain II.
通过对重组受体相关蛋白（RAP）和sortilin结构域进行表面等离子体共振分析，研究了RAP与新鉴定的假定分选受体sortilin的结合，并与它和巨膜蛋白及低密度脂蛋白受体相关蛋白（LRP）的结合进行了比较。数据表明，sortilin中的RAP结合位点位于与酵母液泡蛋白分选10蛋白（Vps10p）同源的富含半胱氨酸的腔内部分，而RAP中的sortilin结合位点位于RAP三个同源结构域的羧基末端结构域III中。sortilin仅结合RAP结构域III，而巨膜蛋白和LRP结合所有RAP结构域，其功能亲和力顺序为：结构域III＞结构域I＞结构域II。
