指抗病毒蛋白质复合体的功能解剖学
Jennifer A Bohn1, Jennifer L Meagher2, Matthew A Takata1
1Laboratory of Retrovirology, The Rockefeller University, New York, NY, 10065, USA.
Nature communications
|December 31, 2024
概括
指抗病毒蛋白 (ZAP) 和它的辅因子TRIM25和KHNYN形成了一个抗病毒复合体. 这项研究揭示了它们的功能解剖学,导致了新型仿真抗病毒蛋白的设计.
科学领域:
- 病毒学 病毒学
- 分子生物学分子生物学
- 免疫学 免疫学 免疫学
背景情况:
- 指抗病毒蛋白 (ZAP) 针对基于CpG含量的病毒RNA.
- 尚不清楚ZAP辅因子TRIM25和KHNYN的作用.
研究的目的:
- 阐明ZAP抗病毒复合体的功能相互作用和域要求.
- 描述KHNYN的酶活性.
- 研究ZAP-辅助因子相互作用的结构基础.
主要方法:
- 使用多个领域的蛋白质相互作用研究.
- 对TRIM25多元化的分析.
- 核酶活动测定KHNYN.
- 在ZAP N端RNA结合域的X射线晶体学.
主要成果:
- TRIM25多元化增强了ZAP活动和特异性.
- KHNYN是一种活性核酶,与N4BP1.1部分冗余.
- ZAP N-终端RNA结合域对于复杂活动至关重要.
- 晶体结构揭示了 KHNYN 相互作用部位远离 RNA 结合.
结论:
- 介绍了ZAP,TRIM25和KHNYN的详细功能解剖学.
- 人工嵌合蛋白显示出复制的抗病毒功能.
- 提出了一个ZAP复杂RNA识别和作用的模型.
相关概念视频
Protein Complex Assembly
10.6K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
10.6K
Protein Complexes with Interchangeable Parts
2.5K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.5K
Assembly of Signaling Complexes
5.7K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
5.7K
Conservation of Protein Domains Over Different Proteins
10.8K
Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
10.8K
Viral Structure
61.7K
Viruses are extraordinarily diverse in shape and size, but they all have several structural features in common. All viruses have a core that contains a DNA- or RNA-based genome. The core is surrounded by a protective coat of proteins called the capsid. The capsid is composed of subunits called capsomeres. The capsid and genome-containing core are together known as the nucleocapsid.
61.7K
Conserved Binding Sites
4.2K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
4.2K


