8omd: Difference between revisions

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'''Unreleased structure'''


The entry 8omd is ON HOLD  until Paper Publication
==Crystal structure of mKHK in complex with compound-4==
<StructureSection load='8omd' size='340' side='right'caption='[[8omd]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8omd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8OMD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8OMD 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=VTJ:compound'>VTJ</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=8omd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8omd OCA], [https://pdbe.org/8omd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8omd RCSB], [https://www.ebi.ac.uk/pdbsum/8omd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8omd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0J9YU79_MOUSE A0A0J9YU79_MOUSE]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A molecular understanding of the proteins involved in fructose metabolism is essential for controlling the current spread of fructose-related obesity, diabetes and related adverse metabolic states in Western populations. Fructose catabolism starts with the phosphorylation of D-fructose to fructose 1-phosphate by ketohexokinase (KHK). KHK exists in two alternatively spliced isoforms: the hepatic and intestinal isoform KHK-C and the peripheral isoform KHK-A. Here, the structure of apo murine KHK (mKHK), which differs from structures of human KHK in overall conformation, is reported. An isoform-selective ligand, which offers a 50-fold higher potency on mKHK and human KHK-A compared with KHK-C, is further characterized. In mKHK, large-scale conformational changes are observed upon ligand binding. The structures suggest a combined strategy for the design of species- and isoform-selective KHK inhibitors.


Authors: Ebenhoch, R., Pautsch, A.
Crystal structures of human and mouse ketohexokinase provide a structural basis for species- and isoform-selective inhibitor design.,Ebenhoch R, Bauer M, Romig H, Gottschling D, Kley JT, Heine N, Weber A, Uphues I, Nar H, Pautsch A Acta Crystallogr D Struct Biol. 2023 Oct 1. doi: 10.1107/S2059798323006137. PMID:37712434<ref>PMID:37712434</ref>


Description: Crystal structure of mKHK in complex with compound-4
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Pautsch, A]]
<div class="pdbe-citations 8omd" style="background-color:#fffaf0;"></div>
[[Category: Ebenhoch, R]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Ebenhoch R]]
[[Category: Pautsch A]]
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