Neprilysin

spinqualitylabelsall models Structure of glycosylated human neprilysin extracellular domain complex with phosphoramidon and Zn+2 ion (grey) (PDB entry 1dmt) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Neprilysin (NEP), also known as neutral endopeptidase, is a Zn-dependent metalloprotease which degrades small secreted peptides like the beta-amyloid peptide, tachykinin, neurotensin and enkephalins. NEP turns off peptide signaling events at the cell surface. NEP is found in brain tissue and is an integral membrane protein. Relevance NEP signaling has also been implicated in cardiovascular disease. NEP level increases in Alzheimer's disease patients. NEP inhibitors like Sacubitril and Sacubitril/valsartan are tested as analgesics and anti-hypertensive agents. Structural highlights A tetrahedrally coordinated Zn atom interacts with the NEP inhibitor and is involved in the catalysis. Active site. Water molecules are shown as red spheres. 3D structures of neprilysin Updated on 21-January-2024 6gid - hNEP extracellular domain 52-750 - human 6sh1 - hNEP extracellular domain (mutant) 6sh2 - hNEP extracellular domain (mutant) + natriuretic peptide 1dmt – hNEP extracellular domain + Zn + phosphoramidon 4cth - hNEP extracellular domain (mutant) + Zn + phosphoramidon 5jmy - hNEP extracellular domain + subitril 1r1h, 1r1i, 1r1j, 1y8j, 2qpj, 2yb9, 6suk, 6svy, 6thp, 6xvp - hNEP extracellular domain + Zn + inhibitor 2yvc – NEP cytoplasmic tail + radixin - mouse 4xbh - rNEP - rabbit 4zr5 - rNEP + phosphoramidon 5v48 - rNEP + thiorphan

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