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首页> 外文期刊>Journal of Molecular Biology >Crystal structure of P58(IPK) TPR fragment reveals the mechanism for its molecular chaperone activity in UPR.
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Crystal structure of P58(IPK) TPR fragment reveals the mechanism for its molecular chaperone activity in UPR.

机译：P58（IPK）TPR片段的晶体结构揭示了其在UPR中分子伴侣活性的机制。

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摘要

P58(IPK) might function as an endoplasmic reticulum molecular chaperone to maintain protein folding homeostasis during unfolded protein responses. P58(IPK) contains nine tetratricopeptide repeat (TPR) motifs and a C-terminal J-domain within its primary sequence. To investigate the mechanism by which P58(IPK) functions to promote protein folding within the endoplasmic reticulum, we have determined the crystal structure of P58(IPK) TPR fragment to 2.5 A resolution by the SAD method. The crystal structure of P58(IPK) revealed three domains (I-III) with similar folds and each domain contains three TPR motifs. An ELISA assay indicated that P58(IPK) acts as a molecular chaperone by interacting with misfolded proteins such as luciferase and rhodanese. The P58(IPK) structure reveals a conserved hydrophobic patch located in domain I that might be involved in binding the misfolded polypeptides. Structure-based mutagenesis for the conserved hydrophobic residues located in domain I significantly reduced the molecular chaperone activity of P58(IPK).
机译：P58（IPK）可能起内质网分子伴侣的作用，在未折叠的蛋白质反应过程中维持蛋白质折叠的稳态。 P58（IPK）在其一级序列中包含九个四肽重复（TPR）基序和一个C端J结构域。为了研究P58（IPK）促进内质网内蛋白质折叠的功能机理，我们通过SAD方法确定了P58（IPK）TPR片段的晶体结构为2.5 A的分辨率。 P58（IPK）的晶体结构显示三个结构域（I-III）具有相似的折叠，每个结构域包含三个TPR基序。 ELISA分析表明，P58（IPK）通过与错误折叠的蛋白质（如萤光素酶和罗丹犬）相互作用而充当分子伴侣。 P58（IPK）结构揭示了位于域I中的一个保守的疏水补丁，可能参与结合错误折叠的多肽。位于结构域I中的保守疏水残基的基于结构的诱变显着降低了P58（IPK）的分子伴侣活性。

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