Properties of the major Zn<sup>2+</sup>-binding site of human alpha-fetoprotein, a potential foetal plasma zinc carrier
The foetal plasma protein α-fetoprotein (AFP) harbours a high-affinity zinc binding site that is likely involved in transport and delivery of essential zinc during foetal development. Based on a recent electron microscopy structure of AFP and aided by biophysical studies on an AFP-derived peptide, we present a refined 5-coordinate model for this site.
Authors
- Claudia A. Blindauer (ORCID: https://orcid.org/0000-0001-8396-9332)
- Jin Lü (ORCID: https://orcid.org/0000-0003-0905-0736)
- Stephen J. Hierons
- Rémi Fritzen (ORCID: https://orcid.org/0000-0003-3457-8364)
- Alan J. Stewart (ORCID: https://orcid.org/0000-0003-4580-1840)
- Swati Arya (ORCID: https://orcid.org/0000-0001-7978-9507)
- Sirilata Polepalli (ORCID: https://orcid.org/0000-0003-1802-4310)
- Siavash Khazaipoul
Institutions
- University of St Andrews (GB)
- University of Warwick (GB)
Publication Details
- Journal
- Chemical Communications
- Published
- 2024-12-27
- DOI
- https://doi.org/10.1039/d4cc06611a
- Citations
- 1
- Primary Topic
- Trace Elements in Health
- Type
- article
- Field-Weighted Citation Impact
- 0.31
Funders
- Leverhulme Trust
- Biotechnology and Biological Sciences Research Council