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Article

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

Molecular & cellular proteomics : MCP - 1 Jan 2021

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

Abstract excerpt

Human α2-macroglobulin (A2M) is the most characterized protease inhibitor in the alpha-macroglobulin (αM) superfamily, but the structure of its native conformation has not been determined. Here, we combined negative stain electron microscopy (EM), small-angle X-ray scattering (SAXS), and cross-linking-mass spectrometry (XL-MS) to investigate native A2M and its collapsed conformations that are obtained through...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

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

Genes

A2M

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