3dwb: Difference between revisions

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{{Seed}}
[[Image:3dwb.jpg|left|200px]]


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==structure of human ECE-1 complexed with phosphoramidon==
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<StructureSection load='3dwb' size='340' side='right'caption='[[3dwb]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3dwb]] 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=3DWB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DWB FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.38&#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=5HD:5-(2-HYDROXYETHYL)NONANE-1,9-DIOL'>5HD</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>
{{STRUCTURE_3dwb|  PDB=3dwb  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3dwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dwb OCA], [https://pdbe.org/3dwb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dwb RCSB], [https://www.ebi.ac.uk/pdbsum/3dwb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dwb ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/ECE1_HUMAN ECE1_HUMAN] Defects in ECE1 are a cause of Hirschsprung disease cardiac defects and autonomic dysfunction (HSCRCDAD) [MIM:[https://omim.org/entry/613870 613870]. It is a form of Hirschsprung disease with skip-lesions defects, craniofacial abnormalities and other dysmorphic features, and autonomic dysfunction.<ref>PMID:9915973</ref>
== Function ==
[https://www.uniprot.org/uniprot/ECE1_HUMAN ECE1_HUMAN] Converts big endothelin-1 to endothelin-1.<ref>PMID:9396733</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dw/3dwb_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=3dwb ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Endothelin-converting enzyme I (ECE-1) is a mammalian type II integral membrane zinc-containing endopeptidase. ECE-1 catalyzes the final step in the biosynthesis of endothelins in a rate-limiting fashion, through post-translational conversion of the biologically inactive big endothelins. Endothelin-1 overproduction has been implicated in a heterogeneous list of diseases including systemic and pulmonary hypertension, stroke and asthma, cardiac and renal failure. Therefore, ECE-1 is a prime therapeutic target for the regulation of endothelin-1 production in vivo and there is considerable interest in selective inhibitors of this enzyme. Here, we present the crystal structure of the extracellular domain (residues 90-770) of human ECE-1 (C428S) with the generic metalloprotease inhibitor phosphoramidon determined at 2.38 A resolution. The structure is closely related to that of human NEP, providing essential information for a detailed understanding of ligand-binding, specificity determinants as well as selectivity criteria. Selective inhibitors of ECE-1s should have beneficial effects for the treatment of diseases in which an overproduction of ETs plays a pathogenic role.


===structure of human ECE-1 complexed with phosphoramidon===
Structure of human endothelin-converting enzyme I complexed with phosphoramidon.,Schulz H, Dale GE, Karimi-Nejad Y, Oefner C J Mol Biol. 2009 Jan 9;385(1):178-87. Epub 2008 Nov 1. PMID:18992253<ref>PMID:18992253</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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(as it appears on PubMed at http://www.pubmed.gov), where 18992253 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_18992253}}
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</StructureSection>
==Disease==
Known disease associated with this structure: Hirschsprung disease, cardiac defects, and autonomic dysfunction OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600423 600423]], Hypertension, essential, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600423 600423]]
 
==About this Structure==
3DWB is a 1 chain 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=3DWB OCA].
 
==Reference==
Structure of human Endothelin-converting Enzyme I Complexed with Phosphoramidon., Schulz H, Dale GE, Karimi-Nejad Y, Oefner C, J Mol Biol. 2008 Nov 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18992253 18992253]
[[Category: Endothelin-converting enzyme 1]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Oefner, C.]]
[[Category: Large Structures]]
[[Category: Alternative splicing]]
[[Category: Oefner C]]
[[Category: Disease mutation]]
[[Category: Glycoprotein]]
[[Category: Hirschsprung disease]]
[[Category: Hydrolase]]
[[Category: Mch_ece_h_25a1_lt1 pdb]]
[[Category: Membrane]]
[[Category: Metal-binding]]
[[Category: Metalloprotease]]
[[Category: Phosphoprotein]]
[[Category: Polymorphism]]
[[Category: Protease]]
[[Category: Protein]]
[[Category: Signal-anchor]]
[[Category: Transmembrane]]
[[Category: Zinc]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Nov 27 13:37:29 2008''
Retrieved from "https://proteopedia.org/3dwb"