5v48
From Proteopedia
Soluble rabbit neprilysin in complex with thiorphan
Structural highlights
FunctionNEP_RABIT Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids. Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9. Involved in the degradation of atrial natriuretic factor (ANF). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers.[UniProtKB:P08473] Publication Abstract from PubMedNeutral 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 A resolution, and bound to the inhibitors phosphoramidon and thiorphan at 2.8 and 3.0 A 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. Structures of soluble rabbit neprilysin complexed with phosphoramidon or thiorphan.,Labiuk SL, Sygusch J, Grochulski P Acta Crystallogr F Struct Biol Commun. 2019 Jun 1;75(Pt 6):405-411. doi:, 10.1107/S2053230X19006046. Epub 2019 May 10. PMID:31204686[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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