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首页> 外文期刊>Biochemistry >IDENTIFYING AND CHARACTERIZING A STRUCTURAL DOMAIN OF PROTEIN DISULFIDE ISOMERASE
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IDENTIFYING AND CHARACTERIZING A STRUCTURAL DOMAIN OF PROTEIN DISULFIDE ISOMERASE

机译：蛋白质二硫键异构酶的结构域的鉴定和表征

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摘要

Protein disulfide isomerase (PDI) appears on the basis of its primary structure to be a multidomain protein, but the number and nature of the domains has been uncertain. Two of the domains, a and a', which are homologous to thioredoxin and active in catalysis of disulfide bond formation, have been identified and characterized previously. Sections of the N-terminal half of the PDI sequence have been expressed and the limits of their folded structures delineated by limited proteolysis. In addition to the a-domain, the boundaries of a domain with no activity on thiol/disulfide groups, designated b, have been identified. This domain has been produced independently; its cooperative unfolding transition and its CD and NMR spectra confirm that it is an autonomously folded structure in isolation and when part of PDI. Fusion of the b-domain to the a-domain, as occurs naturally in the first half of PDI. did not alter substantially the catalytic activity of the a-domain. It still catalyzes only a subset of the thiol/disulfide exchange reactions of intact PDI and has a reduced ability to catalyze protein disulfide rearrangements. The a- and b-domains account structurally for virtually all of the first half of the PDI polypeptide chain, and it is very unlikely that there exists a proposed third domain homologous to the estrogen receptor. The b-domain exhibits some sequence homology to calsequestrin, a calcium binding protein from the sarcoplasmic reticulum of muscle.
机译：蛋白质二硫键异构酶（PDI）在其一级结构的基础上似乎是一个多域蛋白，但域的数量和性质尚不确定。先前已经鉴定和表征了与硫氧还蛋白同源并且在催化二硫键形成中有活性的两个结构域a和a'。已经表达了PDI序列N末端一半的部分，并通过有限的蛋白水解作用描述了其折叠结构的极限。除a结构域外，还鉴定了对硫醇/二硫键基团无活性的结构域的边界，标记为b。该域是独立产生的;它的协同展开过渡及其CD和NMR谱图证实，它是独立存在且属于PDI时的自主折叠结构。 b域与a域的融合，就像在PDI的前半部分自然发生的那样。基本上没有改变α-结构域的催化活性。它仍然仅催化完整PDI的硫醇/二硫键交换反应的一部分，并且催化二硫键蛋白重排的能力降低。 a结构域和b结构域实际上构成了PDI多肽链前半部分的结构，因此，不太可能存在提议的与雌激素受体同源的第三结构域。该b结构域与Calsequestrin（一种来自肌肉肌浆网的钙结合蛋白）具有某些序列同源性。

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