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Function of human Rh based on structure of RhCG at 2.1 Å

By Franz Gruswitz, Sarika Chaudhary, Joseph D. Ho, Avner Schlessinger, Bobak Pezeshki, Chi-Min Ho, Andrej Sali, Connie M. Westhoff and Robert M. Stroud

Abstract

In humans, NH3 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 Å 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 NH3 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

Topics: Biological Sciences
Publisher: National Academy of Sciences
OAI identifier: oai:pubmedcentral.nih.gov:2906887
Provided by: PubMed Central
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