1j37: Difference between revisions
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<StructureSection load='1j37' size='340' side='right'caption='[[1j37]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='1j37' size='340' side='right'caption='[[1j37]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1j37]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1j37]] is a 2 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=1J37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J37 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=X8Z:L-CAPTOPRIL'>X8Z</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=1j37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j37 OCA], [https://pdbe.org/1j37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j37 RCSB], [https://www.ebi.ac.uk/pdbsum/1j37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j37 ProSAT]</span></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=1j37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j37 OCA], [https://pdbe.org/1j37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j37 RCSB], [https://www.ebi.ac.uk/pdbsum/1j37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j37 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[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> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Drosophila melanogaster]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kim HM]] | |||
[[Category: Kim | [[Category: Lee H]] | ||
[[Category: Lee | [[Category: Lee J-O]] | ||
[[Category: Lee | [[Category: Shin DR]] | ||
[[Category: Shin | [[Category: Yoo OJ]] | ||
[[Category: Yoo | |||
Latest revision as of 02:41, 28 December 2023
Crystal Structure of Drosophila AnCECrystal Structure of Drosophila AnCE
Structural highlights
FunctionACE_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.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAngiotensin I-converting enzymes (ACEs) are zinc metallopeptidases that cleave carboxy-terminal dipeptides from short peptide hormones. We have determined the crystal structures of AnCE, a Drosophila homolog of ACE, with and without bound inhibitors to 2.4 A resolution. AnCE contains a large internal channel encompassing the entire protein molecule. This substrate-binding channel is composed of two chambers, reminiscent of a peanut shell. The inhibitor and zinc-binding sites are located in the narrow bottleneck connecting the two chambers. The substrate and inhibitor specificity of AnCE appears to be determined by extensive hydrogen-bonding networks and ionic interactions in the active site channel. The catalytically important zinc ion is coordinated by the conserved Glu395 and histidine residues from a HExxH motif. Crystal structure of Drosophila angiotensin I-converting enzyme bound to captopril and lisinopril.,Kim HM, Shin DR, Yoo OJ, Lee H, Lee JO FEBS Lett. 2003 Mar 13;538(1-3):65-70. PMID:12633854[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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