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Modelling the human rhesus proteins: Implications for structure and function

Conroy, Matthew J.; Bullough, Per A.; Merrick, Mike; Avent, Neil D.


Matthew J. Conroy

Per A. Bullough

Mike Merrick

Neil D. Avent


The mammalian rhesus (Rh) proteins that carry the Rh blood group antigens of red blood cells are related to the ammonium channel (Amt) proteins found in both pro- and eukaryotes. However, despite their clinical importance the structure of the Rh antigens is presently unknown. We have constructed homology models of the human Rh proteins, RhD and RhAG using the structure of the Escherichia coli ammonia channel AmtB as a template, together with secondary structure predictions and the extensive available biochemical data for the Rh proteins. These models suggest that RhAG and the homologous non-erythrocyte Rhesus glycoproteins, RhBG and RhCG, have a very similar channel architecture to AmtB. By comparison, RhD and RhCE have a different arrangement of residues, indicating that if they function as ammonia channels at all, they must do so by a different mechanism. The E. coli AmtB protein is a homotrimer and our models provoke a reassessment of the widely accepted tetrameric model of the organisation of the erythrocyte Rh complex. A critical analysis of previously published data, together with sequencing yield data, lead us to suggest that the erythrocyte Rh complex could indeed also be trimeric. © 2005 Blackwell Publishing Ltd.


Conroy, M. J., Bullough, P. A., Merrick, M., & Avent, N. D. (2005). Modelling the human rhesus proteins: Implications for structure and function. British Journal of Haematology, 131(4), 543-551.

Journal Article Type Article
Publication Date Nov 1, 2005
Journal British Journal of Haematology
Print ISSN 0007-1048
Electronic ISSN 1365-2141
Publisher Wiley
Peer Reviewed Peer Reviewed
Volume 131
Issue 4
Pages 543-551
Keywords rhesus protein, homology model, ammonium transport, oligomeric state, membrane complex
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