9THO
Crystal structure of the adduct formed upon reaction of [V(IV)O(acetylacetonate)2] with human serum transferrin with Fe(III) bound at the C-lobe only
This is a non-PDB format compatible entry.
Summary for 9THO
| Entry DOI | 10.2210/pdb9tho/pdb |
| Descriptor | Serotransferrin, BICARBONATE ION, GLYCEROL, ... (7 entities in total) |
| Functional Keywords | protein metalation, vanadium compounds, metal transport |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 76500.66 |
| Authors | Paolillo, M.,Ferraro, G.,Banneville, A.S.,Cornaciu, I.,Pica, A.,Merlino, A. (deposition date: 2025-12-03, release date: 2026-01-28) |
| Primary citation | Banneville, A.S.,Lucignano, R.,Paolillo, M.,Cuomo, V.,Chino, M.,Ferraro, G.,Picone, D.,Garribba, E.,Cornaciu-Hoffmann, I.,Pica, A.,Merlino, A. First crystal structure of an adduct formed upon reaction of a vanadium compound with human serum transferrin. Commun Chem, 2026 Cited by PubMed Abstract: The interaction of vanadium compounds of pharmaceutical interest with metal-transport proteins like human serum transferrin (hTF) is poorly understood. Direct structural evidence identifying vanadium binding sites on hTF is still lacking. Here, the X-ray structure of the adduct formed when the potential drug [VO(acac)], with acac = acetylacetonato, reacts with human serum transferrin with Fe bound at the C-lobe only (Fe-hTF) has been solved and compared with new structures of Fe-hTF used as controls. Structural analysis revealed the presence of a [VO] anion that can be described as a divanadate(V) anion, [VO], that has one oxygen replaced by the phenolate oxygen of Tyr188. The two vanadium centers adopt tetrahedral geometry, consistent with V behavior. The binding does not alter the overall conformation of Fe-hTF that retains the open conformation of the N-lobe and the closed conformation of the C-lobe, remaining able to be recognized by the transferrin receptor. PubMed: 41545537DOI: 10.1038/s42004-026-01891-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
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