Institute of Neuropathology, University Medical Center Hamburg-Eppendorf, Martinistraße 52, 20251 Hamburg, Germany.
European Molecular Biology Laboratory (EMBL), Hamburg c/o German Electron Synchrotron (DESY), Notkestraße 85, 22607 Hamburg, Germany.
Biochim Biophys Acta Mol Cell Res. 2022 Jun;1869(6):119240. doi: 10.1016/j.bbamcr.2022.119240. Epub 2022 Feb 19.
The prion protein is a multifunctional protein that exists in at least two different folding states. It is subject to diverse proteolytic processing steps that lead to prion protein fragments some of which are membrane-bound whereas others are soluble. A multitude of ligands bind to the prion protein and besides proteinaceous binding partners, interaction with metal ions and nucleic acids occurs. Although of great importance, information on structural and functional consequences of prion protein binding to its partners is limited. Here, we will reflect on the structure-function relationship of the prion protein and its binding partners considering the different folding states and prion protein fragments.
朊病毒蛋白是一种多功能蛋白,至少存在两种不同的折叠状态。它经历多种蛋白水解加工步骤,导致形成朊病毒蛋白片段,其中一些是膜结合的,而另一些是可溶性的。许多配体与朊病毒蛋白结合,除了蛋白质结合伙伴外,还与金属离子和核酸相互作用。尽管具有重要意义,但关于朊病毒蛋白与其结合伙伴结合的结构和功能后果的信息是有限的。在这里,我们将考虑朊病毒蛋白及其结合伙伴的不同折叠状态和朊病毒蛋白片段,来反思朊病毒蛋白的结构-功能关系。