2021
DOI: 10.3390/biom11040505
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Analysis of the Dynamic Proteasome Structure by Cross-Linking Mass Spectrometry

Abstract: The 26S proteasome is a macromolecular complex that degrades proteins maintaining cell homeostasis; thus, determining its structure is a priority to understand its function. Although the 20S proteasome’s structure has been known for some years, the highly dynamic nature of the 19S regulatory particle has presented a challenge to structural biologists. Advances in cryo-electron microscopy (cryo-EM) made it possible to determine the structure of the 19S regulatory particle and showed at least seven different con… Show more

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Cited by 2 publications
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“…Finally, Marta L. Mendes and Gunnar Dittmar [12] describe how cross-linking mass spectrometry (CLMS) is now routinely used in integrative structural biology studies, and it promises to take integrative structural biology to the next level, answering some of the questions about the structure of the 19S regulatory particle and on the different conformational states of the 26S proteasome that have not yet found a definitive answer through cryo-electron microscopy (cryo-EM).…”
mentioning
confidence: 99%
“…Finally, Marta L. Mendes and Gunnar Dittmar [12] describe how cross-linking mass spectrometry (CLMS) is now routinely used in integrative structural biology studies, and it promises to take integrative structural biology to the next level, answering some of the questions about the structure of the 19S regulatory particle and on the different conformational states of the 26S proteasome that have not yet found a definitive answer through cryo-electron microscopy (cryo-EM).…”
mentioning
confidence: 99%