9p6q
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Mouse Ketohexokinase-A without ligand== | |
| + | <StructureSection load='9p6q' size='340' side='right'caption='[[9p6q]], [[Resolution|resolution]] 1.37Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9p6q]] is a 1 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=9P6Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9P6Q 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]] 1.37Å</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=9p6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9p6q OCA], [https://pdbe.org/9p6q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9p6q RCSB], [https://www.ebi.ac.uk/pdbsum/9p6q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9p6q ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Ketohexokinase (KHK) catalyses the initial step in fructose metabolism, converting the furanose form of D-fructose to fructose 1-phosphate in an ATP-dependent reaction. Given its central role in metabolic pathways, KHK has emerged as a target for pharmacological intervention in the treatment of non-alcoholic fatty liver disease, metabolic syndrome, type 2 diabetes and obesity. KHK exists as two isoforms, A and C, which arise from alternative splicing of exon 3, resulting in a differing 45-amino-acid sequence within the 298-amino-acid primary structure of the enzyme. KHK is a biological homodimer, with each subunit adopting an alpha/beta-fold architecture that interlocks with a beta-clasp domain. In the case of KHK-C at least two distinct conformations of the beta-clasp domain have been identified, whereas this conformational flexibility had not been observed in KHK-A. Here, X-ray crystallographic structural investigations of unliganded murine KHK-A refined to 1.37 A resolution revealed the adoption of two conformations similar to those adopted by the human ortholog, suggesting that this structural feature is conserved across species. The functional significance of these conformational changes in KHK-A is of particular interest as this isoform has been implicated in cancer metastasis through a ;moonlighting' protein kinase activity. Understanding the mechanistic role of conformational shifts in KHK-A may provide insights into its broader physiological functions and therapeutic potential. | ||
| - | + | Conformational changes in ketohexokinase are conserved across isozymes and species.,Bae SY, Allen KN, Tolan DR Acta Crystallogr F Struct Biol Commun. 2025 Nov 1;81(Pt 11):451-458. doi: , 10.1107/S2053230X25008428. Epub 2025 Oct 10. PMID:41070915<ref>PMID:41070915</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 9p6q" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Allen KN]] | ||
| + | [[Category: Bae S]] | ||
| + | [[Category: Tolan DR]] | ||
Current revision
Mouse Ketohexokinase-A without ligand
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