4E36

Crystal structure of the human Endoplasmic Reticulum Aminopeptidase 2 variant N392K

Summary for 4E36

• Entry DOI: 10.2210/pdb4e36/pdb
• Related: 3SE6
• Descriptor: Endoplasmic reticulum aminopeptidase 2, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-4)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• Functional Keywords: thermolysin-like catalytic domain, hydrolase, aminopeptidase, zinc binding, glycosylation, endoplasmic reticulum
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 226783.30

Authors

Birtley, J.R.,Saridakis, E.,Pegias, P.,Stratikos, E.,Mavridis, I.M. (deposition date: 2012-03-09, release date: 2012-08-29, Last modification date: 2023-09-13)

• Primary citation: 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.; A common single nucleotide polymorphism in endoplasmic reticulum aminopeptidase 2 induces a specificity switch that leads to altered antigen processing.; J.Immunol., 189:2383-2392, 2012; PubMed: 22837489; DOI: 10.4049/jimmunol.1200918

Experimental method

X-RAY DIFFRACTION (3.22 Å)