Localisation of the C1q binding site within C1q receptor/calreticulin
Localisation of the C1q binding site within C1q receptor/calreticulin
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DOI：
10.1016/s0014-5793(96)01156-8
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发表时间：
1996-11-18
期刊：
影响因子：
3.5
通讯作者：
Schwaeble, WJ
中科院分区：
文献类型：
--
作者：
Stuart, GR;Lynch, NJ;Schwaeble, WJ
C1q 受体（C1qR/collectin 受体）位于多种细胞类型上，Clq 与这些细胞的结合会引发多种反应。蛋白质测序表明，C1qR 与钙网蛋白 (CaR) 几乎相同，钙网蛋白是一种丰富的多功能蛋白，放射性碘标记的 C1qR 和 CaR 与 C1q 结合具有相同的特性。使用 Thiofusion 系统表达三个重组 C1qR/CaR 结构域（N 端结构域、C 端结构域和中央 P 结构域），并用于研究与 C1q 的相互作用。N 结构域和 P 结构域均参与 C1q 结合，A 区域（称为 S 结构域）跨越 N 和 P 交叉点被表达，并显示出与 C1q 的浓度依赖性结合，证明 C1q 结合位点位于该区域内。
C1q receptor (C1qR/collectin receptor) is located on many cell types, Binding of Clq to these cells elicits numerous responses, Protein sequencing has shown that C1qR is almost identical to calreticulin (CaR), an abundant multifunctional protein, Radioiodinated C1qR and CaR bind to C1q with identical characteristics. Three recombinant C1qR/CaR domains (N-, C-terminal domains and central P-domain) were expressed using the Thiofusion system, and used to study the interaction with C1q, Both the N- and P-domains were implicated in C1q binding, A region, termed the S-domain, spanning the N and P intersection was expressed, and showed concentration-dependent binding to C1q, demonstrating that the C1q binding site lies within this region.