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Literature DB >> 20457942

Function of human Rh based on structure of RhCG at 2.1 A.

Franz Gruswitz¹, Sarika Chaudhary, Joseph D Ho, Avner Schlessinger, Bobak Pezeshki, Chi-Min Ho, Andrej Sali, Connie M Westhoff, Robert M Stroud.

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.

Entities: Chemical Gene Species

Mesh：

Substances：

Year: 2010 PMID： 20457942 PMCID： PMC2906887 DOI： 10.1073/pnas.1003587107

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

56 in total

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