Purification, crystallization, and preliminary X-ray diffraction data analysis for PB1 dimer of P62/SQSTM1
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- Purification, crystallization, and preliminary X-ray diffraction data analysis for PB1 dimer of P62/SQSTM1
- Ho Chul Shin; Dahwan Lim; Bonsu Ku; Seung Jun Kim
- Bibliographic Citation
- Biodesign, vol. 6, no. 4, pp. 100-102
- Publication Year
- Autophagy is a degradation pathway that targets many cellular components and plays a particularly important role in protein degradation and recycling. This process is very complex and several proteins participate in this process. One of them, P62/SQSTM1, is related to the N-end rule and induces protein degradation through autophagy. The P62/SQSTM1 makes a huge oligomer, and this oligomerization is known to play an important role in its mechanism. This oligomerization takes two steps. First, the PB1 domain of P62/SQSTM1 makes the base oligomer, and then, when the ligand binds to the ZZ domain of P62/SQSTM1, it induces a higher oligomer by the disulfide bond of the two cysteines. To understand the oligomerization mechanism of P62/SQSTM1, we need to know the dimerization of the PB1 domain. In this study, crystals of PB1 dimer were made and the crystals were diffracted by X-ray to collect usable data up to 3.2A. We are analyzing the structure using the molecular replacement (MR) method.
- Korea Soc-Assoc-Inst
- Appears in Collections:
- Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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