 |
PDBsum entry 4zr5
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Hydrolase
|
|
|
Title:
|
|
Soluble rabbit neprilysin in complex with phosphoramidon
|
|
Structure:
|
|
Neprilysin. Chain: a, b. Synonym: atriopeptidase,enkephalinase,neutral endopeptidase 24.11, neutral endopeptidase,skin fibroblast elastase,sfe. Engineered: yes
|
|
Source:
|
|
Oryctolagus cuniculus. Rabbit. Organism_taxid: 9986. Gene: mme. Expressed in: pichia pastoris. Expression_system_taxid: 4922. Expression_system_variant: his4-
|
|
Resolution:
|
|
|
2.80Å
|
R-factor:
|
0.194
|
R-free:
|
0.227
|
|
|
Authors:
|
|
S.L.Labiuk,P.Grochulski,J.Sygusch
|
|
Key ref:
|
|
S.L.Labiuk
et al.
(2019).
Structures of soluble rabbit neprilysin complexed with phosphoramidon or thiorphan.
Acta Crystallogr F Struct Biol Commun,
75,
405-411.
PubMed id:
DOI:
|
|
|
Date:
|
|
|
11-May-15
|
Release date:
|
08-Jun-16
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
P08049
(NEP_RABIT) -
Neprilysin from Oryctolagus cuniculus
|
|
|
|
Seq:
Struc:
|
|
|
|
750 a.a.
696 a.a.*
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
 |
CATH domain |
|
|
*
PDB and UniProt seqs differ
at 4 residue positions (black
crosses)
|
|
|
|
|
|
|
|
|
|
|
|
|
Enzyme class:
|
|
E.C.3.4.24.11
- neprilysin.
|
|
|
|
|
|
|
Reaction:
|
|
Preferential cleavage at the amino group of hydrophobic residues in insulin, casein, hemoglobin, and a number of other proteins and polypeptides.
|
|
|
|
|
|
Cofactor:
|
|
Zn(2+)
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
Acta Crystallogr F Struct Biol Commun
75:405-411
(2019)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Structures of soluble rabbit neprilysin complexed with phosphoramidon or thiorphan.
|
|
S.L.Labiuk,
J.Sygusch,
P.Grochulski.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
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.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Links
