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兔组氨酸三联体核苷酸结合蛋白1(rHINT1)-腺苷复合物的高分辨率X射线结构,分辨率为1.10 Å。

High-resolution X-ray structure of the rabbit histidine triad nucleotide-binding protein 1 (rHINT1)-adenosine complex at 1.10 Å resolution.

作者信息

Dolot Rafał, Ozga Magdalena, Krakowiak Agnieszka, Nawrot Barbara

机构信息

Department of Bioorganic Chemistry, Centre of Molecular and Macromolecular Studies of the Polish Academy of Sciences, Łódź, Poland.

出版信息

Acta Crystallogr D Biol Crystallogr. 2011 Jul;67(Pt 7):601-7. doi: 10.1107/S0907444911015605. Epub 2011 Jun 14.

Abstract

Histidine triad nucleotide-binding protein 1 (HINT1) represents the most ancient and widespread branch in the histidine-triad protein superfamily. HINT1 plays an important role in various biological processes and has been found in many species. Here, the first complete structure of the rabbit HINT1-adenosine complex is reported at 1.10 Å resolution, which is one of the highest resolutions obtained for a HINT1 structure. The final structure has an R(cryst) of 14.25% (R(free) = 16.77%) and the model exhibits good stereochemical qualities. A detailed analysis of the atomic resolution data allowed an update of the details of the protein structure in comparison to previously published data.

摘要

组氨酸三联体核苷酸结合蛋白1(HINT1)代表了组氨酸三联体蛋白超家族中最古老且分布最广泛的分支。HINT1在多种生物学过程中发挥重要作用,并且已在许多物种中被发现。在此,报道了兔HINT1-腺苷复合物的首个完整结构,分辨率为1.10 Å,这是HINT1结构所获得的最高分辨率之一。最终结构的R(cryst)为14.25%(R(free)=16.77%),且模型具有良好的立体化学性质。与先前发表的数据相比,对原子分辨率数据的详细分析使得蛋白质结构的细节得以更新。

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