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A2ML1 bait region mapping and glycan determination

ABSTRACT: See article for descriptions of the purposes, methods, and results.

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Seandean Harwood

LAB HEAD: Jan J. Enghild

PROVIDER: PXD032010 | Pride | 2022-06-09

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	20210316_NSN_L1.pdResult	Other
	20210316_NSN_L1.raw	Raw
	20210316_NSN_L1_CatG.pdResult	Other
	20210316_NSN_L1_CatG.raw	Raw
	20210316_NSN_L1_Chymo.pdResult	Other

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1 - 5 of 19

Publications

Cryo-EM structures of human A2ML1 elucidate the protease-inhibitory mechanism of the A2M family.

Nielsen Nadia Sukusu NS Zarantonello Alessandra A Harwood Seandean Lykke SL Jensen Kathrine Tejlgård KT Kjøge Katarzyna K Thøgersen Ida B IB Schauser Leif L Karlsen Jesper Lykkegaard JL Andersen Gregers R GR Enghild Jan J JJ

Nature communications 20220531 1

A2ML1 is a monomeric protease inhibitor belonging to the A2M superfamily of protease inhibitors and complement factors. Here, we investigate the protease-inhibitory mechanism of human A2ML1 and determine the structures of its native and protease-cleaved conformations. The functional inhibitory unit of A2ML1 is a monomer that depends on covalent binding of the protease (mediated by A2ML1's thioester) to achieve inhibition. In contrast to the A2M tetramer which traps proteases in two internal cham ...[more]

PMID: 35641520

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