4BB9
Crystal structure of glucokinase regulatory protein complexed to fructose-1-phosphate
Summary for 4BB9
| Entry DOI | 10.2210/pdb4bb9/pdb |
| Related | 4BBA |
| Descriptor | GLUCOKINASE REGULATORY PROTEIN, 1-O-phosphono-beta-D-fructopyranose, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | protein-binding protein, glucose metabolism |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 1 |
| Total formula weight | 70075.21 |
| Authors | 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. (deposition date: 2012-09-21, release date: 2013-05-15, Last modification date: 2024-05-08) |
| Primary citation | 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 Cited by 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: 23621087DOI: 10.1021/BI4000782 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.47 Å) |
Structure validation
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