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Investigating Native Metal Ion Binding Sites in Mammalian Histidine-Rich Glycoprotein
Open accessPublished version of a preprint
Abstract
High Resolution Image Download MS PowerPoint Slide Mammalian histidine-rich glycoprotein (HRG) is a highly versatile and abundant blood plasma glycoprotein with a diverse range of ligands that is involved in regulating many essential biological processes, including coagulation, cell adhesion, and angiogenesis. Despite its biomedical importance, structural information on the multi-domain protein is sparse, not least due to intrinsically disordered regions that elude high-resolution structural characterization. Binding of divalent metal ions, particularly Zn II, to multiple sites within the HRG protein is of critical functional importance and exerts a regulatory role. However, characterization of the Zn II binding sites of HRG is a challenge; their number and composition as well as their affinities and stoichiometries of binding are currently not fully understood. In this study, we explored modern electron paramagnetic resonance (EPR) spectroscopy methods supported by protein secondary and tertiary structure prediction to assemble a holistic picture of native HRG and its interaction with metal ions. To the best of our knowledge, this is the first time that this suite of EPR techniques has been applied to count and characterize endogenous metal ion binding sites in a native mammalian protein of unknown structure.
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Highly accurate protein structure prediction with AlphaFold
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Rolny, C., Mazzone, M., Tugues, S., Laoui, D., Johansson, I., Coulon, C., Squadrito, M. L., Segura, I., Li, X., Knevels, E., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2010.11.009 · Cited by 695
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Metadata
- Authors
- Ackermann, K., Khazaipoul, S., Wort, J. L., Sobczak, A. I. S., Mkami, H. E., Stewart, A. J., & Bode, B. E.
- Affiliations
- University of St Andrews (GB)
- Corresponding author
- Stewart, Alan J.
- Bode, Bela E.
- ORCID
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2023-03-31
- Volume
- 145
- Issue
- 14
- Pages
- 8064-8072
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- PMC
- PMC10103162
- OpenAlex
- W4362460408
- Cited by
- 24
- References
- 2
- Citations by year
- 2026: 6 · 2025: 6 · 2024: 9 · 2023: 3
- FWCI
- 2.91
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of the American Chemical Society (publishedVersion, cc-by)
- ChemRxiv (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- St Andrews Research Repository (St Andrews Research Repository) (submittedVersion, cc-by)
- Funders
- Leverhulme Trust (RPG-2018397)
- British Heart Foundation (FS/15/42/31556, PG/15/9/31270)
- Wellcome Trust (204821/Z/16/Z)
- Biotechnology and Biological Sciences Research Council (BB/R013780/1, BB/T017740/1)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Electron Spin Resonance Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- histidine-rich glycoprotein, metal binding sites, zinc binding, divalent metal ions, intrinsically disordered regions, native protein structure, secondary structure prediction, protein tertiary structure prediction, electron spin resonance, plasma glycoproteins
- MeSH terms
- Histidine-Rich Glycoprotein, Animals, Binding Sites, Blood Coagulation, Glycoproteins, Mammals
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