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Structure paper

TitleConformational dynamics linked to domain closure and substrate binding explain the ERAP1 allosteric regulation mechanism.
Journal, issue, pagesNat Commun, Vol. 12, Page 5302-5302, Year 2021
Publish dateAug 22, 2018 (structure data deposition date)
AuthorsMaben, Z. / Arya, R. / Georgiadis, D. / Stratikos, E. / Stern, L.J.
External linksNat Commun / PubMed:34489420
MethodsX-ray diffraction
Resolution2.92 - 3.31 Å
Structure data

PDB-6m8p:
Human ERAP1 bound to phosphinic pseudotripeptide inhibitor DG013
Method: X-RAY DIFFRACTION / Resolution: 3.31 Å

PDB-6mgq:
ERAP1 in the open conformation bound to 10mer phosphinic inhibitor DG014
Method: X-RAY DIFFRACTION / Resolution: 2.92 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-P52:
Nalpha-[(2S)-2-{[[(1R)-1-amino-3-phenylpropyl](hydroxy)phosphoryl]methyl}-4-methylpentanoyl]-L-tryptophanamide

ChemComp-SO4:
SULFATE ION

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-UNX:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsHYDROLASE/INHIBITOR / Inhibitor / Aminopeptidase / Antigen processing / HYDROLASE / HYDROLASE-INHIBITOR complex / Immune System

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