Function of human Rh based on structure of RhCG at 2.1 A.
basic_science · Level V
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- Record sourced from PubMed, PMID 20457942.
- Also identified by DOI 10.1073/pnas.1003587107 and PMC identifier 2906887.
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Abstract
In humans, NH(3) transport across cell membranes is facilitated by the Rh (rhesus) family of proteins. Human Rh C glycoprotein (RhCG) forms a trimeric complex that plays an essential role in ammonia excretion and renal pH regulation. The X-ray crystallographic structure of human RhCG, determined at 2.1 A resolution, reveals the mechanism of ammonia transport. Each monomer contains 12 transmembrane helices, one more than in the bacterial homologs. Reconstituted into proteoliposomes, RhCG conducts NH(3) to raise internal pH. Models of the erythrocyte Rh complex based on our RhCG structure suggest that the erythrocytic Rh complex is composed of stochastically assembled heterotrimers of RhAG, RhD, and RhCE.
Medical subject headings
- Cation Transport Proteins
- Membrane Glycoproteins
- Rh-Hr Blood-Group System