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Structure paper

TitleMMP activation-associated aminopeptidase N reveals a bivalent 14-3-3 binding motif.
Journal, issue, pagesJ. Biol. Chem., Vol. 295, Page 18266-18275, Year 2020
Publish dateJan 23, 2020 (structure data deposition date)
AuthorsKiehstaller, S. / Ottmann, C. / Hennig, S.
External linksJ. Biol. Chem. / PubMed:33109610
MethodsX-ray diffraction
Resolution1.2 - 1.60000193301 Å
Structure data

PDB-6xwd:
14-3-3 sigma bound to canonical mono-phosphorylated aminopeptidase N (APN, CD13) binding motif
Method: X-RAY DIFFRACTION / Resolution: 1.60000193301 Å

PDB-7aew:
14-3-3 sigma bound to bis-phosphorylated aminopeptidase N (APN, CD13) via canonical and non-canonical binding motifs
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-CA:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-CL:
Unknown entry

Source
  • homo sapiens (human)
KeywordsPROTEIN BINDING / extracellular 14-3-3 Phosphorylation Aminopeptidase N CD13 / PEPTIDE BINDING PROTEIN / extracellular 14-3-3 / phosphorylation / aminopeptidase N / CD13

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