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来自Plasmodium falciparum的P113无特征域的晶体结构

Zhudi Yuan¹, Xiaofang Huang², Lianglei Wang²

¹Department of Urology, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University and Collaborative Innovation Center of Biotherapy, Chengdu 610041, People's Republic of China.

Acta crystallographica. Section D, Structural biology

|April 7, 2025

概括

菌的蛋白质P113将RH5入侵复合体固定在寄生虫表面上. 它的结构显示了保存的螺旋束,这对于杆菌寄生虫入侵机制至关重要.

科学领域:

结构生物学结构生物学
寄生虫学的寄生虫学
分子生物学分子生物学

背景情况:

在红细胞入侵中,Plasmodium falciparum RH5复合体至关重要.
表面蛋白P113将包括CyRPA和RIPR在内的RH5复合体固定在寄生虫表面上.
适当的RH5定位对于宿主细胞进入至关重要.

研究的目的:

阐明P113.3的螺旋结构丰富领域的结构和功能特征.
了解P113在Plasmodium入侵中的分子机制.

主要方法:

P113螺旋式丰富域的表达,净化和结晶.
在1.7 Å分辨率下进行X射线晶体学以确定apo结构.
序列保存分析,STRING蛋白质-蛋白质相互作用分析,以及AlphaFold预测.

主要成果:

P113螺旋丰富的域 (余量311-679) 形成了两个不同的左边直角四螺旋捆.
在感染人类的Plasmodium物种和其他Plasmodium物种中,P113的保存率很高.
P113作为一个枢纽蛋白,与包括RIPR在内的多个合作伙伴相互作用,并确定了特定的结合部位.

结论:

确定的结构为P113.3的分子组织提供了洞察力.
维护P113的结构和相互作用网络对于其在Plasmodium入侵中的功能至关重要.
这项研究促进了对P113在Plasmodium生物学中的作用和潜在的治疗向的理解.

关键词:

在P113中,P113是P113中的一个.原菌 (Plasmodium falciparum) 是一种有毒的病毒.晶体结构晶体结构疟疾疟疾是一种疾病.

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