4BB9

Crystal structure of glucokinase regulatory protein complexed to fructose-1-phosphate

4BB9 の概要

• エントリーDOI: 10.2210/pdb4bb9/pdb
• 関連するPDBエントリー: 4BBA
• 分子名称: GLUCOKINASE REGULATORY PROTEIN, 1-O-phosphono-beta-D-fructopyranose, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: protein-binding protein, glucose metabolism
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 70075.21

構造登録者

Pautsch, A.,Stadler, N.,Loehle, A.,Lenter, M.,Rist, W.,Berg, A.,Glocker, L.,Nar, H.,Reinert, D.,Heckel, A.,Schnapp, G.,Kauschke, S.G. (登録日: 2012-09-21, 公開日: 2013-05-15, 最終更新日: 2024-05-08)

主引用文献

Pautsch, A.,Stadler, N.,Loehle, A.,Rist, W.,Berg, A.,Glocker, L.,Nar, H.,Reinert, D.,Lenter, M.,Heckel, A.,Schnapp, G.,Kauschke, S.G.
Crystal Structure of Glucokinase Regulatory Protein.
Biochemistry, 52:3523-, 2013

PubMed Abstract: Glucokinase (GK) plays a major role in the regulation of blood glucose homeostasis in both the liver and the pancreas. In the liver, GK is controlled by the GK regulatory protein (GKRP). GKRP in turn is activated by fructose 6-phosphate (F6P) and inactivated by fructose 1-phosphate (F1P). Disrupting the GK-GKRP complex increases the activity of GK in the cytosol and is considered an attractive concept for the regulation of blood glucose. We have determined the crystal structure of GKRP in its inactive F1P-bound form. The binding site for F1P is located deeply buried at a domain interface, and H-D exchange experiments confirmed that F1P and F6P compete for this site. The structure of the inactive GKRP-F1P complex provides a starting point for understanding the mechanism of fructose phosphate-dependent GK regulation at an atomic level.

PubMed: 23621087
DOI: 10.1021/BI4000782

実験手法

X-RAY DIFFRACTION (1.47 Å)