6SH1
Crystal structure of substrate-free human neprilysin E584D.
This is a non-PDB format compatible entry.
Summary for 6SH1
| Entry DOI | 10.2210/pdb6sh1/pdb |
| Descriptor | Neprilysin, 2-acetamido-2-deoxy-beta-D-glucopyranose, 1,2-ETHANEDIOL, ... (5 entities in total) |
| Functional Keywords | zinc metalloprotease, neprilysin, neutral endopeptidase., peptide binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 161109.64 |
| Authors | Moss, S.,Subramanian, V.,Acharya, K.R. (deposition date: 2019-08-05, release date: 2019-09-25, Last modification date: 2024-11-13) |
| Primary citation | Moss, S.,Subramanian, V.,Acharya, K.R. Crystal structure of peptide-bound neprilysin reveals key binding interactions. Febs Lett., 594:327-336, 2020 Cited by PubMed Abstract: Neprilysin (NEP) is a promiscuous zinc metalloprotease with broad substrate specificity and cleaves a remarkable diversity of substrates through endopeptidase action. Two of these - amyloid-β and natriuretic peptides - implicate the enzyme in both Alzheimer's disease and cardiovascular disease, respectively. Here, we report the creation of a catalytically inactive NEP (E584D) to determine the first peptide-bound crystal structure at 2.6 Å resolution. The structure reveals key interactions involved in substrate binding which we have identified to be conserved in other known zinc metalloproteases. In addition, the structure provides evidence for a potential exosite within the central cavity that may play a critical role in substrate positioning. Together, these results contribute to our understanding of the molecular function of NEP. PubMed: 31514225DOI: 10.1002/1873-3468.13602 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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