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9HQ6

Structural insights in the HuHf@gold-monocarbene adduct: aurophilicity revealed in a biological context

9HQ6 の概要
エントリーDOI10.2210/pdb9hq6/pdb
EMDBエントリー52339
分子名称Ferritin heavy chain, 1-butyl-3-methyl-1H-imidazol-3-ium, GOLD ION, ... (4 entities in total)
機能のキーワードiron, gold, metal transport, metal storage, anticancer drugs, drug nanocarrier, metal binding protein
由来する生物種Homo sapiens (human)
タンパク質・核酸の鎖数24
化学式量合計529237.08
構造登録者
主引用文献Cosottini, L.,Giachetti, A.,Guerri, A.,Martinez-Castillo, A.,Geri, A.,Zineddu, S.,Abrescia, N.G.A.,Messori, L.,Turano, P.,Rosato, A.
Structural Insight Into a Human H Ferritin@Gold-Monocarbene Adduct: Aurophilicity Revealed in a Biological Context.
Angew.Chem.Int.Ed.Engl., :e202503778-e202503778, 2025
Cited by
PubMed Abstract: Human H ferritin (HuHf) has excellent potential as a nanocarrier for the selective delivery of anticancer metal-based drugs to tumor cells. Here, we addressed the interaction of the gold monocarbene compound Au(NHC)Cl with HuHf by electrospray ionization-mass spectrometry (ESI-MS) measurements, which provide the metalation state of the protein subunits and demonstrate the involvement of protein cysteines in gold binding. The adduct between Au(NHC)Cl and HuHf was studied by cryo-EM measurements, resulting in a high-resolution 3D density map at 1.51 Å. The cryo-EM structure shows a novel tetranuclear gold(I) cluster, located in a surface pocket of each subunit where it is bound to Cys90 and Cys102. The short inter-metal distances are diagnostic of the occurrence of aurophilic interactions. The present work demonstrates the usefulness of cryo-EM to investigate the interactions between metal-based drugs and their protein targets/carriers, also leveraging the strong signal of transition metal ions.
PubMed: 40249912
DOI: 10.1002/anie.202503778
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (1.51 Å)
構造検証レポート
Validation report summary of 9hq6
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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