TAILIEUCHUNG - Báo cáo khoa học: An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein

The interaction between the human copper(I) chaperone, HAH1, and one of its two physiological partners, the Menkes disease protein (ATP7A), was investigated in solution using heteronuclear NMR. The study was carried out through titrations involving HAH1 and either the second or the fifth soluble domains of ATP7A (MNK2 and MNK5, respectively), in the pres-ence of copper(I). The copper-transfer properties of MNK2 and MNK5 are similar, and differ significantly from those previously observed for the yeast homologous system. . | ềFEBS Journal An NMR study of the interaction between the human copper I chaperone and the second and fifth metal-binding domains of the Menkes protein Lucia Banci1 2 Ivano Bertini1 2 Simone Ciofi-Baffoni1 2 Christos T Chasapis1 3 Nick Hadjiliadis3 and Antonio Rosato1 2 1 Magnetic Resonance Center CERM University of Florence Italy 2 Department of Chemistry University of Florence Italy 3 Section of Inorganic and AnalyticalChemistry Department of Chemistry University of Ioannina Greece Keywords copper I metal homeostasis metallochaperone protein-protein interaction Correspondence I. Bertini Magnetic Resonance Center University of Florence Via L. Sacconi 6 50019 Sesto Fiorentino Italy Fax 39 055-457-4271 Tel 39 055-457-4272 E-mail ivanobertini@ Received 30 September 2004 revised 30 November 2004 accepted 13 December 2004 doi The interaction between the human copper I chaperone HAH1 and one of its two physiological partners the Menkes disease protein ATP7A was investigated in solution using heteronuclear NMR. The study was carried out through titrations involving HAH1 and either the second or the fifth soluble domains of ATP7A MNK2 and MNK5 respectively in the presence of copper I . The copper-transfer properties of MNK2 and MNK5 are similar and differ significantly from those previously observed for the yeast homologous system. In particular no stable adduct is formed between either of the MNK domains and HAH1. The copper I transfer reaction is slow on the time scale of the NMR chemical shift and the equilibrium is significantly shifted towards the formation of copper I -MNK2 MNK5. The solution structures of both apo- and copper I -MNK5 which were not available are also reported. The results are discussed in comparison with the data available in the literature for the interaction between HAH1 and its partners from other spectroscopic techniques. Copper an essential trace metal is utilized as a cofactor in a variety of .

• Báo cáo khoa học
• Report medicine
• traditional medicine
• scientific reports
• Antimicrobial
• cell structure
• genetics
• medical knowledge
• medical research
• analysis of cytoplasmic
• oxidation
• Crystal structure
• bacteria
• hemoglobin
• medicine
• cell proliferation
• breast cancer
• chemical reaction
• gastric cancer
• hormone medicine
• tumor cells
• biochemical studies
• environmental medicine