Structures of soluble rabbit neprilysin complexed with phosphoramidon or thiorphan
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.
Source: Acta Crystallographica Section F - Category: Biochemistry Authors: Labiuk, S.L. Sygusch, J. Grochulski, P. Tags: neutral endopeptidase neprilysin phosphoramidon thiorphan research communications Source Type: research
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