1dmt

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[[Image:1dmt.gif|left|200px]]
 
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==STRUCTURE OF HUMAN NEUTRAL ENDOPEPTIDASE COMPLEXED WITH PHOSPHORAMIDON==
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The line below this paragraph, containing "STRUCTURE_1dmt", creates the "Structure Box" on the page.
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<StructureSection load='1dmt' size='340' side='right'caption='[[1dmt]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1dmt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DMT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DMT FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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>
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{{STRUCTURE_1dmt| PDB=1dmt | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dmt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dmt OCA], [https://pdbe.org/1dmt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dmt RCSB], [https://www.ebi.ac.uk/pdbsum/1dmt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dmt ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NEP_HUMAN NEP_HUMAN] 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.<ref>PMID:2531377</ref> <ref>PMID:15283675</ref> <ref>PMID:20876573</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dm/1dmt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dmt ConSurf].
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<div style="clear:both"></div>
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'''STRUCTURE OF HUMAN NEUTRAL ENDOPEPTIDASE COMPLEXED WITH PHOSPHORAMIDON'''
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==See Also==
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*[[Neprilysin|Neprilysin]]
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== References ==
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==Overview==
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<references/>
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Neutral endopeptidase is a mammalian type II integral membrane zinc-containing endopeptidase, which degrades and inactivates a number of bioactive peptides. The range of substrates cleaved by neutral endopeptidase in vitro includes the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor. Due to the physiological importance of neutral endopeptidase in the modulation of nociceptive and pressor responses there is considerable interest in inhibitors of this enzyme as novel analgesics and anti-hypertensive agents. Here we describe the crystal structure of the extracellular domain (residues 52-749) of human NEP complexed with the generic metalloproteinase inhibitor phosphoramidon at 2.1 A resolution. The structure reveals two multiply connected folding domains which embrace a large central cavity containing the active site. The inhibitor is bound to one side of this cavity and its binding mode provides a detailed understanding of the ligand-binding and specificity determinants.
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__TOC__
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</StructureSection>
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==About this Structure==
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1DMT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DMT OCA].
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==Reference==
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Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon., Oefner C, D'Arcy A, Hennig M, Winkler FK, Dale GE, J Mol Biol. 2000 Feb 18;296(2):341-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10669592 10669592]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Neprilysin]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: D'Arcy A]]
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[[Category: Arcy, A D.]]
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[[Category: Dale GE]]
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[[Category: Dale, G E.]]
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[[Category: Hennig M]]
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[[Category: Hennig, M.]]
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[[Category: Oefner C]]
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[[Category: Oefner, C.]]
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[[Category: Winkler FK]]
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[[Category: Winkler, F K.]]
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[[Category: Hydrolase]]
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[[Category: Metalloprotease]]
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[[Category: Signal-anchor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:02:12 2008''
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Current revision

STRUCTURE OF HUMAN NEUTRAL ENDOPEPTIDASE COMPLEXED WITH PHOSPHORAMIDON

PDB ID 1dmt

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