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

Harwood SL, Lyngsø J, Zarantonello A, Kjøge K, Nielsen PK, Andersen GR, Pedersen JS, Enghild JJ
Mol Cell Proteomics 20:100090 (2021 May 6)

PMID: 33964423 doi: 10.1016/j.mcpro.2021.100090

Submitted to SASBDB: 2020 May 29 Published in SASBDB: 2021 Jun 15

SASDJK3 – Native alpha-2-macroglobulin, glycosylated Sample: Alpha-2-macroglobulin tetramer, 643 kDa Homo sapiens protein Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4 Experiment: SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2020 Jan 22 RgGuinier 7.7 nm Dmax 22.7 nm

SASDJL3 – Methylamine-treated alpha-2-macroglobulin, glycosylated Sample: Alpha-2-macroglobulin tetramer, 643 kDa Homo sapiens protein Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4 Experiment: SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2020 Jan 22 RgGuinier 6.7 nm Dmax 19.7 nm

SASDJM3 – Trypsin-treated alpha-2-macroglobulin, glycosylated Sample: Cationic trypsin dimer, 52 kDa Bos taurus protein Alpha-2-macroglobulin tetramer, 643 kDa Homo sapiens protein Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4 Experiment: SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2020 Jan 15 RgGuinier 6.6 nm Dmax 19.7 nm

SASDJN3 – Native alpha-2-macroglobulin, deglycosylated Sample: Alpha-2-macroglobulin tetramer, 643 kDa Homo sapiens protein Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4 Experiment: SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2019 Apr 12 RgGuinier 7.6 nm Dmax 20.2 nm

SASDJP3 – Methylamine-treated alpha-2-macroglobulin, deglcycosylated Sample: Alpha-2-macroglobulin tetramer, 643 kDa Homo sapiens protein Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4 Experiment: SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2019 Apr 13 RgGuinier 6.6 nm Dmax 19.7 nm

SASDJQ3 – Trypsin-treated alpha-2-macroglobulin, deglycosylated Sample: Cationic trypsin dimer, 52 kDa Bos taurus protein Alpha-2-macroglobulin tetramer, 643 kDa Homo sapiens protein Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4 Experiment: SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2020 Jan 22 RgGuinier 6.6 nm Dmax 20.7 nm