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. 2017 Feb 3;284(10):1473–1488. doi: 10.1111/febs.14009

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© 2017 Federation of European Biochemical Societies

This article is being made freely available through PubMed Central as part of the COVID-19 public health emergency response. It can be used for unrestricted research re-use and analysis in any form or by any means with acknowledgement of the original source, for the duration of the public health emergency.

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Structure and conservation of M1 aminopeptidases. (A) X‐ray crystal structure of human aminopeptidase N (APN) 7 colored according to domains with domain I in teal, domain II in orange, domain III in magenta, and domain IV in blue. (B) Crystallographically observed dimer of APN, that is also proposed to occur on the cell surface membrane 7 to which APN is attached via domain I (teal). Domains colored as in A. (C–E) Characteristic structures of M1 aminopeptidases colored according to sequence conservation (high degree of conservation in purple, average in white, and low in cyan). Sequence alignments and conservation calculations performed using ConSurf http://consurf.tau.ac.il/2016/ 83): (C) the M1 aminopeptidase from P. falciparum (PfA‐M1) 27, (D) human endoplasmic reticulum aminopeptidase 1 (ERAP1) 75, (E) human leukotriene A4 hydrolase (LTA4H) 6.