Gruswitz Franz, Chaudhary Sarika, Ho Joseph D, Schlessinger Avner, Pezeshki Bobak, Ho Chi-Min, Sali Andrej, Westhoff Connie M, Stroud Robert M
Department of Biochemistry and Biophysics, S412C Genentech Hall, Center for the Structure of Membrane Proteins, and Membrane Protein Expression Center, University of California, San Francisco, CA 94158, USA.
Proc Natl Acad Sci U S A. 2010 May 25;107(21):9638-43. doi: 10.1073/pnas.1003587107. Epub 2010 May 10.
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.
在人类中,NH(3)跨细胞膜的转运由Rh(恒河猴)蛋白家族介导。人类Rh C糖蛋白(RhCG)形成三聚体复合物,在氨排泄和肾脏pH调节中起重要作用。以2.1埃分辨率测定的人类RhCG的X射线晶体结构揭示了氨转运的机制。每个单体包含12个跨膜螺旋,比细菌同源物多一个。重组到蛋白脂质体中后,RhCG传导NH(3)以提高内部pH。基于我们的RhCG结构建立的红细胞Rh复合物模型表明,红细胞Rh复合物由RhAG、RhD和RhCE的随机组装异源三聚体组成。