4ca8: Difference between revisions

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<StructureSection load='4ca8' size='340' side='right'caption='[[4ca8]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
<StructureSection load='4ca8' size='340' side='right'caption='[[4ca8]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ca8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CA8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CA8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ca8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CA8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CA8 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3ES:[(2S)-2-({3-[HYDROXYL(2-PHENYL-(1R)-1-{[(BENZYLOXY)[(2S)-2-({3-[HYDROXYL(2-PHENYL-(1R)-1-CARBONYL]-AMINO}ETHYL)PHOSPHINYL]-2-[(3-PHENYLISOXAZOL-5-YL)METHYL]-1-OXO-PROPYL}AMINO)-3-(4-HYDROXY-PHENYL)'>3ES</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3ES:[(2S)-2-({3-[HYDROXYL(2-PHENYL-(1R)-1-{[(BENZYLOXY)[(2S)-2-({3-[HYDROXYL(2-PHENYL-(1R)-1-CARBONYL]-AMINO}ETHYL)PHOSPHINYL]-2-[(3-PHENYLISOXAZOL-5-YL)METHYL]-1-OXO-PROPYL}AMINO)-3-(4-HYDROXY-PHENYL)'>3ES</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ca5|4ca5]], [[4ca6|4ca6]], [[4ca7|4ca7]]</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=4ca8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ca8 OCA], [https://pdbe.org/4ca8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ca8 RCSB], [https://www.ebi.ac.uk/pdbsum/4ca8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ca8 ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidyl-dipeptidase_A Peptidyl-dipeptidase A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.15.1 3.4.15.1] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ca8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ca8 OCA], [http://pdbe.org/4ca8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ca8 RCSB], [http://www.ebi.ac.uk/pdbsum/4ca8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ca8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ACE_DROME ACE_DROME]] May be involved in the specific maturation or degradation of a number of bioactive peptides. May play a role in the contractions of the heart, gut and testes, and in spermatid differentiation.<ref>PMID:12591244</ref> 
[[https://www.uniprot.org/uniprot/ACE_DROME ACE_DROME]] May be involved in the specific maturation or degradation of a number of bioactive peptides. May play a role in the contractions of the heart, gut and testes, and in spermatid differentiation.<ref>PMID:12591244</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human somatic angiotensin-I converting enzyme (ACE) is a zinc-dependent dipeptidyl carboxypeptidase and a central component of the renin angiotensin-aldosterone system (RAAS). Its involvement in the modulation of physiological actions of peptide hormones has positioned ACE as an important therapeutic target for the treatment of hypertension and cardiovascular disorders. Here, we report the crystal structures of the two catalytic domains of human ACE (N- and C-) in complex with FI, the S enantiomer of the phosphinic ACE/ECE-1 (endothelin converting enzyme) dual inhibitor FII, to a resolution of 1.91A and 1.85 A, respectively. In addition, we have determined the structure of AnCE (an ACE homologue from Drosophila melanogaster) in complex with both isomers. The inhibitor FI (S configuration) can adapt to the active site of ACE catalytic domains and shows key differences in its binding mechanism mostly through the reorientation of the isoxazole phenyl side group at the P1 ' position, compared to FII (R configuration). Differences in binding are also observed between FI and FII in complex with AnCE. Thus, the new structures of the ACE-inhibitor complexes presented here provide useful information for further exploration of ACE inhibitor pharmacophores involving phosphinic peptides and illustrate the role of chirality in enhancing drug specificity. This article is protected by copyright. All rights reserved.
 
Crystal structures of highly specific phosphinic tripeptide enantiomers in complex with the angiotensin-I converting enzyme.,Masuyer G, Akif M, Czarny B, Beau F, Schwager SL, Sturrock ED, Isaac RE, Dive V, Acharya KR FEBS J. 2013 Nov 29. doi: 10.1111/febs.12660. PMID:24289879<ref>PMID:24289879</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ca8" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Drome]]
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Peptidyl-dipeptidase A]]
[[Category: Acharya KR]]
[[Category: Acharya, K R]]
[[Category: Akif M]]
[[Category: Akif, M]]
[[Category: Beau F]]
[[Category: Beau, F]]
[[Category: Czarny B]]
[[Category: Czarny, B]]
[[Category: Dive V]]
[[Category: Dive, V]]
[[Category: Isaac RE]]
[[Category: Isaac, R E]]
[[Category: Masuyer G]]
[[Category: Masuyer, G]]
[[Category: Schwager SLU]]
[[Category: Schwager, S L.U]]
[[Category: Sturrock ED]]
[[Category: Sturrock, E D]]
[[Category: Hydrolase]]
[[Category: Inhibitor binding]]
[[Category: Zinc metallopeptidase]]

Revision as of 17:34, 7 September 2022

Drosophila Angiotensin converting enzyme (AnCE) in complex with a phosphinic tripeptide FII

4ca8, resolution 1.99Å

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