一个PDZ双重重复折叠并通过不同的路径展开
Valeria Pennacchietti1, Sara di Matteo1, Livia Pagano1
1Dipartimento di Scienze Biochimiche "A. Rossi Fanelli," Sapienza Università di Roma, Laboratory affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, Rome, Italy.
Protein science : a publication of the Protein Society
|November 18, 2024
概括
这项研究揭示了X11 PDZ1-PDZ2合重复的独特蛋白质折叠和展开路径. 它在不同的实验条件下调和了蛋白质折叠动力学的明显矛盾.
科学领域:
- 生物化学 生化学
- 结构生物学 结构生物学
- 蛋白质动力学 蛋白质动力学
背景情况:
- 蛋白质折叠和展开的实验传统上假定微观的可逆性,折叠和展开是反向的过程.
- 这种假设适用于单域蛋白质,但对于表现出不可逆转的展开的复杂蛋白质,通常是失败的.
- 具有不可逆转展开的复杂蛋白质通常被认为不适合折叠动力学研究.
研究的目的:
- 在不同的实验条件下研究蛋白质折叠和展开的途径.
- 调和可逆性的理论假设和复杂蛋白质的实验观测之间的差异.
- 证明折叠动力学研究对具有潜在不可逆转展开的蛋白质的适用性.
主要方法:
- 使用X11 PDZ1-PDZ2串联重复作为一个模型系统.
- 在各种条件下进行蛋白质折叠和展开实验.
- 分析折叠和展开路径以确定差异.
主要成果:
- 观察到X11 PDZ1-PDZ2合重复的明显折叠和展开路径.
- 证明不同的实验条件导致不同的途径.
- 展示了复杂的蛋白质可以表现出不同的途径,挑战了简单可逆性的假设.
结论:
- X11 PDZ1-PDZ2 串联重复显示了取决于条件的折叠和展开路径.
- 复杂蛋白质展开的明显不可逆转性可以通过在各种条件下考虑不同的途径来协调.
- 折叠动力学研究可以通过考虑通路复杂性来应用于复杂蛋白质.
更多相关视频
相关概念视频
Restarting Stalled Replication Forks
5.8K
DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart,...
5.8K
Mechanism of Filopodia Formation
2.3K
Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
2.3K
Intrinsically Disordered Proteins
17.7K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
17.7K
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
Mechanism of Lamellipodia Formation
2.5K
Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
2.5K
The Unfolded Protein Response
4.4K
The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
4.4K


