View source for 4zr5


==Soluble rabbit neprilysin in complex with phosphoramidon==
<StructureSection load='4zr5' size='340' side='right'caption='[[4zr5]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4zr5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZR5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZR5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8016&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=RDF:N-ALPHA-L-RHAMNOPYRANOSYLOXY(HYDROXYPHOSPHINYL)-L-LEUCYL-L-TRYPTOPHAN'>RDF</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4zr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zr5 OCA], [https://pdbe.org/4zr5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zr5 RCSB], [https://www.ebi.ac.uk/pdbsum/4zr5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zr5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NEP_RABIT NEP_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]
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== Publication Abstract from PubMed ==
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 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<ref>PMID:31204686</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4zr5" style="background-color:#fffaf0;"></div>

==See Also==
*[[Neprilysin|Neprilysin]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Grochulski P]]
[[Category: Labiuk SL]]
[[Category: Sygusch J]]