5oae: Difference between revisions
New page: '''Unreleased structure''' The entry 5oae is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures |
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==Crystal Structure of tyrosinase from Bacillus megaterium with SVF inhibitor in the active site== | |||
<StructureSection load='5oae' size='340' side='right'caption='[[5oae]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5oae]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium Priestia megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OAE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OAE 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]] 2.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=SVF:1-[4-[(4-fluorophenyl)methyl]piperidin-1-yl]ethanone'>SVF</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=5oae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oae OCA], [https://pdbe.org/5oae PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oae RCSB], [https://www.ebi.ac.uk/pdbsum/5oae PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oae ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/B2ZB02_PRIMG B2ZB02_PRIMG] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The inhibition of tyrosinase (Ty, EC 1.14.18.1) represents an efficient strategy of decreasing melanogenesis and skin hyperpigmentation. A combination of crystallographic and docking studies on two different tyrosinases, that from Bacillus megaterium (TyBm) and that from a mushroom (TyM), has contributed to increasing our knowledge about their structural information and translating that information to the most druggable human Ty (TyH) isozyme. In particular, we designed and synthesized a series of 1-(4-fluorobenzyl)piperazine and 1-(4-fluorobenzyl)piperidine derivatives showing inhibitory activities on TyM at micromolar ranges and more potency than that of the reference compound, kojic acid. The crystal structures of TyBm with inhibitor 3 (IC50 value of 25.11 muM) and 16 (IC50 value of 5.25 muM) were solved, confirming the binding poses hypothesized by in silico studies and revealing the main molecular determinants for the binding recognition of the inhibitors. | |||
Targeting Tyrosinase: Development and Structural Insights of Novel Inhibitors Bearing Arylpiperidine and Arylpiperazine Fragments.,Ferro S, Deri B, Germano MP, Gitto R, Ielo L, Buemi MR, Certo G, Vittorio S, Rapisarda A, Pazy Y, Fishman A, De Luca L J Med Chem. 2018 Apr 20. doi: 10.1021/acs.jmedchem.7b01745. PMID:29634898<ref>PMID:29634898</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5oae" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Priestia megaterium]] | |||
[[Category: Deri B]] | |||
[[Category: Fishman A]] | |||
[[Category: Gitto R]] | |||
[[Category: Pazy Benhar Y]] | |||
Latest revision as of 12:38, 6 December 2023
Crystal Structure of tyrosinase from Bacillus megaterium with SVF inhibitor in the active siteCrystal Structure of tyrosinase from Bacillus megaterium with SVF inhibitor in the active site
Structural highlights
FunctionPublication Abstract from PubMedThe inhibition of tyrosinase (Ty, EC 1.14.18.1) represents an efficient strategy of decreasing melanogenesis and skin hyperpigmentation. A combination of crystallographic and docking studies on two different tyrosinases, that from Bacillus megaterium (TyBm) and that from a mushroom (TyM), has contributed to increasing our knowledge about their structural information and translating that information to the most druggable human Ty (TyH) isozyme. In particular, we designed and synthesized a series of 1-(4-fluorobenzyl)piperazine and 1-(4-fluorobenzyl)piperidine derivatives showing inhibitory activities on TyM at micromolar ranges and more potency than that of the reference compound, kojic acid. The crystal structures of TyBm with inhibitor 3 (IC50 value of 25.11 muM) and 16 (IC50 value of 5.25 muM) were solved, confirming the binding poses hypothesized by in silico studies and revealing the main molecular determinants for the binding recognition of the inhibitors. Targeting Tyrosinase: Development and Structural Insights of Novel Inhibitors Bearing Arylpiperidine and Arylpiperazine Fragments.,Ferro S, Deri B, Germano MP, Gitto R, Ielo L, Buemi MR, Certo G, Vittorio S, Rapisarda A, Pazy Y, Fishman A, De Luca L J Med Chem. 2018 Apr 20. doi: 10.1021/acs.jmedchem.7b01745. PMID:29634898[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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