1R1H: Structural Analysis Of Neprilysin With Various Specific And Potent Inhibitors

Citation:
Abstract
Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor. Owing to the physiological importance of NEP in the modulation of nociceptive and pressor responses, there is considerable interest in inhibitors of this enzyme as novel analgesics and antihypertensive agents. Here, the crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with various potent and competitive inhibitors are described. The structures unambiguously reveal the binding mode of the different zinc-chelating groups and the subsite specificity of the enzyme.
PDB ID: 1R1HDownload
MMDB ID: 29298
PDB Deposition Date: 2003/9/24
Updated in MMDB: 2007/11
Experimental Method:
x-ray diffraction
Resolution: 1.95  Å
Source Organism:
Similar Structures:
Biological Unit for 1R1H: monomeric; determined by author
Molecular Components in 1R1H
Label Count Molecule
Protein (1 molecule)
1
Neprilysin(Gene symbol: MME)
Molecule annotation
Chemicals (5 molecules)
1
3
2
1
3
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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