Expert Reviews in Molecular Medicine: http://www.expertreviews.org/
DOI: 10.1017/S1462399406010969; 12 June 2006
Neil D. Avent, Tracey E. Madgett, Zoe E. Lee, David J. Head, Deborah G. Maddocks and Lucy H. Skinner (2006) Molecular biology of Rh proteins and relevance to molecular medicine.
Expert Rev. Mol. Med. Vol. 8, Issue 13, DOI: 10.1017/S1462399406010969

Molecular biology of Rh proteins and relevance to molecular medicine

Neil D. Avent, Tracey E. Madgett, Zoe E. Lee, David J. Head, Deborah G. Maddocks and Lucy H. Skinner

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The Rhesus (Rh) blood group system is expressed by a pair of 12-transmembrane-domain-containing proteins, the RhCcEe and RhD proteins. RhCcEe and RhD associate as a Rh core complex that comprises one RhD/CcEe protein and most likely two Rh-associated glycoproteins (RhAG) as a trimer. All these Rh proteins are homologous and share this homology with two human non-erythroid proteins, RhBG and RhCG. All Rh protein superfamily members share homology and function in a similar manner to the Mep/Amt ammonium transporters, which are highly conserved in bacteria, plants and invertebrates. Significant advances have been made in our understanding of the structure and function of Rh proteins, as well as in the clinical management of Rh haemolytic disease. This review summarises our current knowledge concerning the molecular biology of Rh proteins and their role in transfusion and pregnancy incompatibility.

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Figure 1. Genomic organisation of the human RH locus.
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Figure 2. Location of the partial-D-causative amino acid polymorphisms.
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Figure 3. Location of some weak-D-causative amino acid polymorphisms.
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Figure 4. Model of the band 3–Rh protein complex.
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