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8OME

Crystal structure of hKHK-A in complex with compound-4

8OME の概要
エントリーDOI10.2210/pdb8ome/pdb
分子名称Ketohexokinase, compound (3 entities in total)
機能のキーワードketohexokinase, khk, inhibitor bound, sugar kinase, isoform selectivity, sugar binding protein
由来する生物種Homo sapiens (human)
タンパク質・核酸の鎖数4
化学式量合計133019.61
構造登録者
Ebenhoch, R.,Pautsch, A. (登録日: 2023-03-31, 公開日: 2023-09-27, 最終更新日: 2023-10-25)
主引用文献Ebenhoch, R.,Bauer, M.,Romig, H.,Gottschling, D.,Kley, J.T.,Heine, N.,Weber, A.,Uphues, I.,Nar, H.,Pautsch, A.
Crystal structures of human and mouse ketohexokinase provide a structural basis for species- and isoform-selective inhibitor design.
Acta Crystallogr D Struct Biol, 79:871-880, 2023
Cited by
PubMed Abstract: 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.
PubMed: 37712434
DOI: 10.1107/S2059798323006137
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2 Å)
構造検証レポート
Validation report summary of 8ome
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-07-16に公開中

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