3HD6: Crystal Structure of the Human Rhesus Glycoprotein RhCG

Citation:
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.
PDB ID: 3HD6Download
MMDB ID: 76445
PDB Deposition Date: 2009/5/6
Updated in MMDB: 2012/09
Experimental Method:
x-ray diffraction
Resolution: 2.1  Å
Source Organism:
Similar Structures:
Biological Unit for 3HD6: trimeric; determined by author and by software (PISA)
Molecular Components in 3HD6
Label Count Molecule
Proteins (3 molecules)
3
Ammonium Transporter RH Type C(Gene symbol: RHCG)
Molecule annotation
Chemicals (3 molecules)
1
3
* Click molecule labels to explore molecular sequence information.

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