锌离子介导的“天然未折叠”人胸腺素α的结构形成与压缩
Zn(2+)-mediated structure formation and compaction of the "natively unfolded" human prothymosin alpha.
作者信息
Uversky V N, Gillespie J R, Millett I S, Khodyakova A V, Vasilenko R N, Vasiliev A M, Rodionov I L, Kozlovskaya G D, Dolgikh D A, Fink A L, Doniach S, Permyakov E A, Abramov V M
机构信息
Institute for Biological Instrumentation, Russian Academy of Sciences, Pushchino, Moscow Region, 142292, Russia.
出版信息
Biochem Biophys Res Commun. 2000 Jan 19;267(2):663-8. doi: 10.1006/bbrc.1999.2013.
Human recombinant prothymosin alpha (ProTalpha) is known to have coil-like conformation at neutral pH; i.e., it belongs to the class of "natively unfolded" proteins. By means of circular dichroism, SAXS, and ANS fluorescence, we have investigated the effect of several divalent cations on the structure of this protein. Results of these studies are consistent with the conclusion that ProTalpha conformation is unaffected by large excess of Ca(2+), Mg(2+), Mn(2+), Cu(2+), and Ni(2+). However, Zn(2+) induces compaction and considerable rearrangement of the protein structure. This means that ProTalpha can specifically interact with Zn(2+) (K(D) approximately 10(-3) M), and such interactions induce folding of the natively unfolded protein into a compact partially folded (premolten globule-like) conformation. It is possible that these structural changes may be important for the function of this protein.
已知人重组前胸腺素α（ProTα）在中性pH值下具有螺旋状构象；也就是说，它属于“天然未折叠”蛋白类别。通过圆二色性、小角X射线散射和ANS荧光，我们研究了几种二价阳离子对该蛋白结构的影响。这些研究结果与以下结论一致：大量过量的Ca(2+)、Mg(2+)、Mn(2+)、Cu(2+)和Ni(2+)不会影响ProTα的构象。然而，Zn(2+)会诱导蛋白结构的压缩和显著重排。这意味着ProTα可以与Zn(2+)特异性相互作用（解离常数K(D)约为10(-3) M），并且这种相互作用会诱导天然未折叠的蛋白折叠成紧凑的部分折叠（类前熔球）构象。这些结构变化可能对该蛋白的功能很重要。
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