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Mol Cell Proteomics. 2021;20:100090. doi: 10.1016/j.mcpro.2021.100090. Epub 2021 May 06.

Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism.

Molecular & cellular proteomics : MCP

Seandean Lykke Harwood, Jeppe Lyngsø, Alessandra Zarantonello, Katarzyna Kjøge, Peter Kresten Nielsen, Gregers Rom Andersen, Jan Skov Pedersen, Jan J Enghild

Affiliations

  1. Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark; Global Research Technologies, Novo Nordisk A/S, Måløv, Denmark.
  2. Interdisciplinary Nanoscience Center, Aarhus University, Aarhus, Denmark; Department of Chemistry, Aarhus University, Aarhus, Denmark.
  3. Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark.
  4. Global Research Technologies, Novo Nordisk A/S, Måløv, Denmark.
  5. Interdisciplinary Nanoscience Center, Aarhus University, Aarhus, Denmark; Department of Chemistry, Aarhus University, Aarhus, Denmark. Electronic address: [email protected].
  6. Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark; Interdisciplinary Nanoscience Center, Aarhus University, Aarhus, Denmark. Electronic address: [email protected].

PMID: 33964423 PMCID: PMC8167298 DOI: 10.1016/j.mcpro.2021.100090

Abstract

Human α

Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.

Keywords: alpha 2 macroglobulin; alpha-macroglobulins; conformational change; electron microscopy; macroglobulins; protease inhibitor; protein conformation; protein cross-linking; small-angle X-ray scattering; structural model

Conflict of interest statement

Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.

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