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TitleA common single nucleotide polymorphism in endoplasmic reticulum aminopeptidase 2 induces a specificity switch that leads to altered antigen processing.
Journal, issue, pagesJ. Immunol., Vol. 189, Page 2383-2392, Year 2012
Publish dateMar 9, 2012 (structure data deposition date)
AuthorsEvnouchidou, I. / Birtley, J. / Seregin, S. / Papakyriakou, A. / Zervoudi, E. / Samiotaki, M. / Panayotou, G. / Giastas, P. / Petrakis, O. / Georgiadis, D. ...Evnouchidou, I. / Birtley, J. / Seregin, S. / Papakyriakou, A. / Zervoudi, E. / Samiotaki, M. / Panayotou, G. / Giastas, P. / Petrakis, O. / Georgiadis, D. / Amalfitano, A. / Saridakis, E. / Mavridis, I.M. / Stratikos, E.
External linksJ. Immunol. / PubMed:22837489
MethodsX-ray diffraction
Resolution3.22 Å
Structure data

PDB-4e36:
Crystal structure of the human Endoplasmic Reticulum Aminopeptidase 2 variant N392K
Method: X-RAY DIFFRACTION / Resolution: 3.22 Å

Chemicals

ChemComp-LYS:
LYSINE

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

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / Thermolysin-like catalytic domain / Aminopeptidase / Zinc binding / Glycosylation / Endoplasmic Reticulum

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