8omg: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of mKHK (apo)== | |||
<StructureSection load='8omg' size='340' side='right'caption='[[8omg]], [[Resolution|resolution]] 1.82Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8omg]] is a 2 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=8OMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8OMG 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]] 1.82Å</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=8omg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8omg OCA], [https://pdbe.org/8omg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8omg RCSB], [https://www.ebi.ac.uk/pdbsum/8omg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8omg ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/KHK_MOUSE KHK_MOUSE] Catalyzes the phosphorylation of the ketose sugar fructose to fructose-1-phosphate.[UniProtKB:P50053] | |||
<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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Ebenhoch | <div class="pdbe-citations 8omg" style="background-color:#fffaf0;"></div> | ||
[[Category: Pautsch | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Ebenhoch E]] | |||
[[Category: Pautsch P]] | |||
