3HD6

Crystal Structure of the Human Rhesus Glycoprotein RhCG

3HD6 の概要

• エントリーDOI: 10.2210/pdb3hd6/pdb
• 関連するPDBエントリー: 1u7g 2b2h 2ns1 3B9W 3B9Z 3BHS
• 分子名称: Ammonium transporter Rh type C, octyl beta-D-glucopyranoside (3 entities in total)
• 機能のキーワード: ammonia, channel, rhesus, glycoprotein, transporter, membrane, structural genomics, psi-2, protein structure initiative, center for structures of membrane proteins, csmp, ammonia transport, cell membrane, transmembrane, transport, membrane protein, transport protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 54470.96

構造登録者

Gruswitz, F.,Chaudhary, S.,Ho, J.D.,Pezeshki, B.,Ho, C.-M.,Stroud, R.M.,Center for Structures of Membrane Proteins (CSMP) (登録日: 2009-05-06, 公開日: 2009-09-01, 最終更新日: 2023-09-06)

主引用文献

Gruswitz, F.,Chaudhary, S.,Ho, J.D.,Schlessinger, A.,Pezeshki, B.,Ho, C.M.,Sali, A.,Westhoff, C.M.,Stroud, R.M.
Function of human Rh based on structure of RhCG at 2.1 A.
Proc.Natl.Acad.Sci.USA, 107:9638-9643, 2010

PubMed 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.

PubMed: 20457942
DOI: 10.1073/pnas.1003587107

実験手法

X-RAY DIFFRACTION (2.1 Å)