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首页> 外文期刊>FEBS Letters >The mouse FKBP23 binds to BiP in ER and the binding of C‐terminal domain is interrelated with Ca2+ concentration
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The mouse FKBP23 binds to BiP in ER and the binding of C‐terminal domain is interrelated with Ca2+ concentration

机译:小鼠FKBP23与ER中的BiP结合并且C末端结构域的结合与Ca2 +浓度相关

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摘要

>FK506 binding protein 23 from mouse (mFKBP23) is a peptidyl-prolyl cis-trans isomerase (PPIase) from the endoplasmic reticulum (ER), which consists of an N-terminal PPIase domain and a C-terminal domain with Ca2+ binding sites. The assay of adsorption from ER extract with glutathione S-transferase-mFKBP23 attached to glutathione-Sepharose 4B shows that mFKBP23 binds to mouse immunoglobulin binding protein (mBiP). The same assay with the recombinant proteins of the N- and C-termini of mFKBP23 shows that the binding of the C-terminus is Ca2+-dependent and the switch point is between 2 and 3 mM. By high concentration of Ca2+ this binding cannot be detected. Furthermore, the Ca2+-regulated binding of mFKBP23 and mBiP in ER can be detected by means of co-immunoprecipitation.
机译:小鼠的> FK506结合蛋白23(mFKBP23)是来自内质网(ER)的肽基脯氨酰顺式-反式异构酶(PPIase),由N末端的PPIase结构域和具有Ca 2 + 结合位点的C末端结构域。谷胱甘肽-Sepharose 4B附着的谷胱甘肽 S -转移酶-mFKBP23对ER提取物的吸附分析表明,mFKBP23与小鼠免疫球蛋白结合蛋白(mBiP)结合。用mFKBP23的N和C末端重组蛋白进行的同一试验表明,C末端的结合是Ca 2 + 依赖性的,转换点在2-3 mM之间。通过高浓度的Ca 2 + 不能检测到这种结合。此外,可以通过共免疫沉淀法检测ER中mFKBP23和mBiP的Ca 2+调节的结合。

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