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TitleSynergy of protease-binding sites within the ecotin homodimer is crucial for inhibition of MASP enzymes and for blocking lectin pathway activation.
Journal, issue, pagesJ. Biol. Chem., Vol. 298, Page 101985-101985, Year 2022
Publish dateSep 17, 2021 (structure data deposition date)
AuthorsNagy, Z.A. / Heja, D. / Bencze, D. / Kiss, B. / Boros, E. / Szakacs, D. / Fodor, K. / Wilmanns, M. / Kocsis, A. / Dobo, J. ...Nagy, Z.A. / Heja, D. / Bencze, D. / Kiss, B. / Boros, E. / Szakacs, D. / Fodor, K. / Wilmanns, M. / Kocsis, A. / Dobo, J. / Gal, P. / Harmat, V. / Pal, G.
External linksJ. Biol. Chem. / PubMed:35483450
MethodsX-ray diffraction
Resolution2.40001520992 - 3.39 Å
Structure data

PDB-7pqn:
Catalytic fragment of MASP-2 in complex with ecotin
Method: X-RAY DIFFRACTION / Resolution: 2.40001520992 Å

PDB-7pqo:
Catalytic fragment of MASP-1 in complex with P1 site mutant ecotin
Method: X-RAY DIFFRACTION / Resolution: 3.39 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

Source
  • escherichia coli (strain k12) (bacteria)
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / serine protease / complement / inhibitor

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