9CXV
Crystal structure of Human FN3K bound with ADP and DMF (I)
This is a non-PDB format compatible entry.
Summary for 9CXV
| Entry DOI | 10.2210/pdb9cxv/pdb |
| Descriptor | Fructosamine-3-kinase, SULFATE ION, MAGNESIUM ION, ... (7 entities in total) |
| Functional Keywords | kinase, transferase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 68427.72 |
| Authors | Garg, A.,On, K.F.,Joshua-Tor, L. (deposition date: 2024-07-31, release date: 2024-12-18, Last modification date: 2025-02-05) |
| Primary citation | Garg, A.,On, K.F.,Xiao, Y.,Elkayam, E.,Cifani, P.,David, Y.,Joshua-Tor, L. The molecular basis of Human FN3K mediated phosphorylation of glycated substrates. Nat Commun, 16:941-941, 2025 Cited by PubMed Abstract: Glycation, a non-enzymatic post-translational modification occurring on proteins, can be actively reversed via site-specific phosphorylation of the fructose-lysine moiety by FN3K kinase, to impact the cellular function of the target protein. A regulatory axis between FN3K and glycated protein targets has been associated with conditions like diabetes and cancer. However, the molecular basis of this relationship has not been explored so far. Here, we determined a series of crystal structures of HsFN3K in the apo-state, and in complex with different nucleotide analogs together with a sugar substrate mimic to reveal the features important for its kinase activity and substrate recognition. Additionally, the dynamics in sugar substrate binding during the kinase catalytic cycle provide important mechanistic insights into HsFN3K function. Our structural work provides the molecular basis for rational small molecule design targeting FN3K. PubMed: 39843453DOI: 10.1038/s41467-025-56207-z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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