5V48

Soluble rabbit neprilysin in complex with thiorphan

Summary for 5V48

• Entry DOI: 10.2210/pdb5v48/pdb
• Related: 4XBH
• Descriptor: Neprilysin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (6 entities in total)
• Functional Keywords: neutral endopeptidase, proteinase, zn-dependent, hydrolase
• Biological source: Oryctolagus cuniculus (Rabbit)
• Total number of polymer chains: 2
• Total formula weight: 161957.40

Authors

Labiuk, S.L.,Grochulski, P.,Sygusch, J. (deposition date: 2017-03-08, release date: 2018-03-14, Last modification date: 2024-10-23)

Primary citation

Labiuk, S.L.,Sygusch, J.,Grochulski, P.
Structures of soluble rabbit neprilysin complexed with phosphoramidon or thiorphan.
Acta Crystallogr.,Sect.F, 75:405-411, 2019

PubMed 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.

PubMed: 31204686
DOI: 10.1107/S2053230X19006046

Experimental method

X-RAY DIFFRACTION (2.9965 Å)