鼻病毒 A28 的皮康宁 3C 的制备和结晶

IF 0.6 4区材料科学 Q4 CRYSTALLOGRAPHY Crystallography Reports Pub Date : 2024-02-05 DOI:10.1134/s1063774523601119

A. E. Tishin, A. V. Gladysheva, L. A. Pyatavina, S. E. Olkin, A. A. Gladysheva, I. R. Imatdionov, A. V. Vlaskina, A. Yu. Nikolaeva, V. R. Samygina, A. P. Agafonov

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引用次数: 0

摘要

摘要人鼻病毒皮卡那霉素 3C 是一种高价值的商用半胱氨酸蛋白酶，被广泛用于纯化目标蛋白时去除亲和标签和融合蛋白。本研究中制备的鼻病毒 A28 picornain 3C 变体在 NCBI 数据库中没有注释，在 PDB 中有 79% 的序列同一性，而且以前没有在蛋白质工程中使用过。我们制定了分离和纯化该蛋白质的方案，以便将其用于结构研究。找到了初始结晶条件。鼻病毒 A28 picornain 3C 结构的确定和分析将为蛋白水解酶进化的基础研究和该蛋白酶最佳变体的设计提供新的可能性。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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Preparation and Crystallization of Picornain 3C of Rhinovirus A28

Abstract

Human rhinovirus picornain 3C is a high-value commercial cysteine protease, which is widely used to remove affinity tags and fusion proteins during the purification of the target proteins. A variant of rhinovirus A28 picornain 3C produced in this study is not annotated in the NCBI databases, shares 79% sequence identity in the PDB, and was not previously used in the protein engineering. A protocol was developed for the isolation and purification of the protein to use it in structural studies. The initial crystallization conditions were found. The determination and analysis of the structure of rhinovirus A28 picornain 3C will provide new possibilities for performing basic research on the evolution of proteolytic enzymes and for the design of the optimal variant of this protease.

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来源期刊

Crystallography Reports 化学-晶体学

CiteScore

1.10

自引率

28.60%

发文量

审稿时长

4-8 weeks

期刊介绍： Crystallography Reports is a journal that publishes original articles short communications, and reviews on various aspects of crystallography: diffraction and scattering of X-rays, electrons, and neutrons, determination of crystal structure of inorganic and organic substances, including proteins and other biological substances; UV-VIS and IR spectroscopy; growth, imperfect structure and physical properties of crystals; thin films, liquid crystals, nanomaterials, partially disordered systems, and the methods of studies.