Neprilysin
From Proteopedia
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- | <StructureSection load='1dmt' size='400' side='right' caption='Structure of glycosylated human neprilysin extracellular domain complex with phosphoramidon (PDB entry [[1dmt]])' scene=''> | + | <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=''> |
== 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. | ||
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== Structural highlights == | == Structural highlights == | ||
- | A tetrahedrally coordinated Zn atom interacts with the NEP inhibitor and is involved in the catalysis<ref>PMID: | + | A tetrahedrally coordinated Zn atom interacts with the NEP inhibitor and is involved in the catalysis<ref>PMID: 10669592</ref>. |
==3D structures of neprilysin== | ==3D structures of neprilysin== |
Revision as of 06:59, 8 May 2016
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