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酪蛋白激酶Iδ的晶体学研究,以深入了解其自身抑制作用的结构。

Crystallographic studies of casein kinase I delta toward a structural understanding of auto-inhibition.

作者信息

Longenecker K L, Roach P J, Hurley T D

机构信息

Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202,USA.

出版信息

Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):473-5. doi: 10.1107/s0907444997011724.

DOI:10.1107/s0907444997011724
PMID:9761932
Abstract

A recombinant form of mammalian casein kinase I delta (CKIdelta) containing the catalytic domain and an auto-inhibitory domain was expressed in Escherichia coli, purified and crystallized. X-ray data were collected to 2.4 A resolution, and the crystals belong to space group C2221. Molecular replacement using the structure of the catalytic domain of CKIdelta yielded strong electron density for residues in the model, but no interpretable density was found for the inhibitory domain. A conserved intermolecular contact suggests the formation of dimers which would inhibit the activity of this protein kinase.

摘要

一种包含催化结构域和自身抑制结构域的重组形式的哺乳动物酪蛋白激酶Iδ(CKIδ)在大肠杆菌中表达、纯化并结晶。收集到分辨率为2.4 Å的X射线数据,晶体属于空间群C2221。使用CKIδ催化结构域的结构进行分子置换,模型中的残基产生了较强的电子密度,但未发现抑制结构域的可解释密度。一种保守的分子间接触表明形成了二聚体,这将抑制这种蛋白激酶的活性。

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