Recent cryogenic electron microscopy structures of human A2M may not be representative of the native protein
Author:
Affiliation:
1. Department of Molecular Biology and Genetics, Aarhus University, 8000 Aarhus, Denmark
Funder
Velux Fonden
Danish council for independent research
Novo Nordisk Foundation
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Link
https://pnas.org/doi/pdf/10.1073/pnas.2210218119
Reference10 articles.
1. Cryo-EM structures show the mechanistic basis of pan-peptidase inhibition by human α2-macroglobulin
2. Structures of complement component C3 provide insights into the function and evolution of immunity
3. Cryo-EM structures of human A2ML1 elucidate the protease-inhibitory mechanism of the A2M family
4. Structural Mechanics of the Alpha-2-Macroglobulin Transformation
5. Spontaneous reformation of the intramolecular thioester in complement protein C3 and low temperature capture of a conformational intermediate capable of reformation.
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1. Proteolytic cleavage of the TGFβ co‐receptor CD109 changes its conformation, resulting in protease inhibition via activation of its thiol ester, and dissociation from the cell membrane;The FEBS Journal;2024-04-08
2. Frozen fresh blood plasma preserves the functionality of native human α2-macroglobulin;Scientific Reports;2023-03-20
3. Reply to Harwood et al.: Alternative functional conformations of native human α 2 -macroglobulin;Proceedings of the National Academy of Sciences;2022-08-16
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