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Updated: Jan 23, 2026

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
Published on: March 6, 2013
Structures of soluble rabbit neprilysin complexed with phosphoramidon or thiorphan
Shaunivan L Labiuk1, Jurgen Sygusch2, Pawel Grochulski1
1Canadian Light Source, 44 Innovation Boulevard, Saskatoon, SK S7N 2V3, Canada.
Abstract:
Neutral endopeptidase (neprilysin; NEP) is a proteinase that cleaves a wide variety of peptides and has been implicated in Alzheimer's disease, cardiovascular conditions, arthritis and other inflammatory diseases. The structure of the soluble extracellular domain (residues 55-750) of rabbit neprilysin was solved both in its native form at 2.1 Å resolution, and bound to the inhibitors phosphoramidon and thiorphan at 2.8 and 3.0 Å resolution, respectively. Consistent with the extracellular domain of human neprilysin, the structure reveals a large central cavity which contains the active site and the location for inhibitor binding.
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