An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal‐binding domains of the Menkes protein
Open accessAbstract
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.
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Kex values for Atox1 and MK2/MK5 are 5-10.
“Moreover, Kex values for Atox1 and MK2/MK5 are 5–10 [19].”
From In Vitro Thermodynamic Dissection of Human Copper Transfer from Chaperone to Target Protein (2012) · cites this paper as [19]
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- Authors
- Banci, L., Bertini, I., Ciofi‐Baffoni, S., Chasapis, C. T., Hadjiliadis, N., & Rosato, A.
- Affiliations
- University of Florence (IT)
- University of Ioannina (GR)
- Corresponding author
- Bertini, Ivano
- ORCID
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2005-01-13
- Volume
- 272
- Issue
- 3
- Pages
- 865-871
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W1884328895
- Cited by
- 59
- References
- 33
- Citations by year
- 2024: 1 · 2023: 2 · 2019: 1 · 2018: 3 · 2017: 2 · 2016: 2 · 2015: 3 · 2014: 1 · 2013: 1 · 2012: 3
- FWCI
- 7.26
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Journal (publishedVersion)
- PubMed (publishedVersion)
- Florence Research (University of Florence) (submittedVersion)
- Funders
- European Commission
- Ente Cassa di Risparmio di Firenze
- Ministero dell’Istruzione, dell’Università e della Ricerca (COFIN-2003, MIUR-COFIN 2003)
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- ATP7A, MNK2, protein-protein interaction, metal-binding domain, solution structure, copper homeostasis
- MeSH terms
- Copper-Transporting ATPases, Copper Transport Proteins, Adenosine Triphosphatases, Binding Sites, Copper, Humans, Models, Molecular, Recombinant Fusion Proteins, Molecular Chaperones, Nuclear Magnetic Resonance, Biomolecular, Cation Transport Proteins, Metallochaperones
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