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Structures of soluble rabbit neprilysin complexed with phosphoramidon or thiorphan.

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.

SUBMITTER: Labiuk SL

PROVIDER: S-EPMC6572095 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature

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Structures of soluble rabbit neprilysin complexed with phosphoramidon or thiorphan.

Labiuk Shaunivan L SL Sygusch Jurgen J Grochulski Pawel P

Acta crystallographica. Section F, Structural biology communications 20190510 Pt 6

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 ...[more]

PMID: 31204686

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