Neprilysin

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<StructureSection load='1dmt' size='400' side='right' caption='Structure of glycosylated human neprilysin extracellular domain complex with phosphoramidon and Zn+2 ion (grey) (PDB entry [[1dmt]])' scene=''>
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<StructureSection load='1dmt' size='400' side='right' caption='Structure of glycosylated human neprilysin extracellular domain complex with phosphoramidon and Zn+2 ion (grey) (PDB entry [[1dmt]])' scene='51/516479/Cv/1'>
== Function ==
== 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.<ref>PMID: 15134871</ref><ref>PMID: 15544569</ref><ref>PMID: 17476590</ref><ref>PMID: 18393807</ref><ref>PMID: 18470479</ref><ref>PMID: 23684647</ref><ref>PMID: 23883611</ref><ref>PMID: 24391587</ref> NEP turns off peptide signaling events at the cell surface. NEP is found in brain tissue and is an integral membrane protein.
'''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.<ref>PMID: 15134871</ref><ref>PMID: 15544569</ref><ref>PMID: 17476590</ref><ref>PMID: 18393807</ref><ref>PMID: 18470479</ref><ref>PMID: 23684647</ref><ref>PMID: 23883611</ref><ref>PMID: 24391587</ref> NEP turns off peptide signaling events at the cell surface. NEP is found in brain tissue and is an integral membrane protein.

Revision as of 06:51, 1 June 2016

Structure of glycosylated human neprilysin extracellular domain complex with phosphoramidon and Zn+2 ion (grey) (PDB entry 1dmt)

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Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Brenton Horne

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