Molecular dynamics simulations of positively selected codons in <scp>FcγRI</scp> reveal novel biochemical binding properties
R substitutions demonstrate an implication for electron conjugation. Examining key sites at this binding FcγRI-IgG interface, our data demonstrate that these two codons have evolved in humans to be relatively insensitive to shifts in pH promoting a more stable interaction with the Fc portion of IgG during diseases that promote acidosis.
Authors
- Amit Nathubhai (ORCID: https://orcid.org/0000-0003-3686-2799)
- Lee R. Machado (ORCID: https://orcid.org/0000-0001-7974-2178)
- Mauricio Cafiero (ORCID: https://orcid.org/0000-0002-4895-1783)
- Jodie Score (ORCID: https://orcid.org/0000-0001-8801-3380)
- Omar Arias‐Gaguancela (ORCID: https://orcid.org/0000-0003-2985-9006)
- Morgan Grainger
- Fiona Gibson
- David A Young
Institutions
- University of Northampton (GB)
- ResearchWorks (United States) (US)
- University of Reading (GB)
Publication Details
- Journal
- FEBS Open Bio
- Published
- 2026-05-01
- DOI
- https://doi.org/10.1002/2211-5463.70247
- Primary Topic
- Monoclonal and Polyclonal Antibodies Research
- Type
- article
- Field-Weighted Citation Impact
- 0.00