9r3z

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Current revision (10:50, 3 September 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9r3z is ON HOLD until 2027-05-06
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==Exploiting ALDH1A2 and ALDH1A3 Isoform Variability for Crystallization Screening==
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<StructureSection load='9r3z' size='340' side='right'caption='[[9r3z]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9r3z]] is a 4 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=9R3Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9R3Z FirstGlance]. <br>
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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]] 2.8&#8491;</td></tr>
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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=9r3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9r3z OCA], [https://pdbe.org/9r3z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9r3z RCSB], [https://www.ebi.ac.uk/pdbsum/9r3z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9r3z ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AL1A2_HUMAN AL1A2_HUMAN] Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Does metabolize octanal and decanal but does not metabolize citral, benzaldehyde, acetaldehyde and propanal efficiently (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Members of the human aldehyde dehydrogenase family 1 (ALDH1As) play a crucial role in converting retinal to retinoic acid, a multifunctional bioactive compound. Most evidence highlight ALDH1As as markers for cancer stem cells correlating with tumour aggressiveness. Increasing structural and biochemical data about these important isoenzymes have been reported in literature. Crystal structures of human ALDH1A2 have been so far only obtained in the presence of ligands/cofactors from vapour diffusion hanging drops. Apo-enzyme structures have been described only for the other two members of the family (ALDH1A1 and ALDH1A3) serving as the basis for their co-crystallisation with various ligands. In this study, we describe the first apo-ALDH1A2 structure obtained from nanolitre sitting-drop crystallisation, which expands the potential for high-throughput structure-based drug discovery studies on this isoform. We also explore the crystallisability of NAD(+)-ALDH1A3 from microlitre drops and compare the structure obtained from it with that of apo-ALDH1A2. Finally, we propose strategies compatible with robotic setups to streamline structural studies on ALDH1A3 and facilitate the exploration of extensive ligand libraries.
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Authors: Garaavglia, S., Mazzorana, M.
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Exploiting ALDH1A2 and ALDH1A3 isoform variability for crystallisation screening.,Siragusa S, Garavaglia S, Mazzorana M Biochem Biophys Res Commun. 2025 Aug 14;780:152469. doi: , 10.1016/j.bbrc.2025.152469. PMID:40829477<ref>PMID:40829477</ref>
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Description: Exploiting ALDH1A2 and ALDH1A3 Isoform Variability for Crystallization Screening
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Mazzorana, M]]
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<div class="pdbe-citations 9r3z" style="background-color:#fffaf0;"></div>
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[[Category: Garaavglia, S]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Garaavglia S]]
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[[Category: Mazzorana M]]

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Exploiting ALDH1A2 and ALDH1A3 Isoform Variability for Crystallization Screening

PDB ID 9r3z

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