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PDBsum entry 3hd6

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protein ligands links
Membrane protein, transport protein PDB id
3hd6
Jmol
Contents
Protein chain
403 a.a. *
Ligands
BOG
Waters ×116
* Residue conservation analysis
PDB id:
3hd6
Name: Membrane protein, transport protein
Title: Crystal structure of the human rhesus glycoprotein rhcg
Structure: Ammonium transporter rh typE C. Chain: a. Synonym: rhesus blood group family typE C glycoprotein, rh typE C glycoprotein, rh typE C glycoprotein, tumor-related drc2, rh glycoprotein kidney. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: c15orf6, cdrc2, pdrc2, rhcg, rhgk. Expressed in: homo sapiens. Expression_system_taxid: 9606.
Resolution:
2.10Å     R-factor:   0.170     R-free:   0.195
Authors: F.Gruswitz,S.Chaudhary,J.D.Ho,B.Pezeshki,C-.M.Ho,R.M.Stroud, For Structures Of Membrane Proteins (Csmp)
Key ref: F.Gruswitz et al. (2010). Function of human Rh based on structure of RhCG at 2.1 A. Proc Natl Acad Sci U S A, 107, 9638-9643. PubMed id: 20457942
Date:
06-May-09     Release date:   01-Sep-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9UBD6  (RHCG_HUMAN) -  Ammonium transporter Rh type C
Seq:
Struc:
479 a.a.
403 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   8 terms 
  Biological process     ammonium transmembrane transport   10 terms 
  Biochemical function     ankyrin binding     2 terms  

 

 
Proc Natl Acad Sci U S A 107:9638-9643 (2010)
PubMed id: 20457942  
 
 
Function of human Rh based on structure of RhCG at 2.1 A.
F.Gruswitz, S.Chaudhary, J.D.Ho, A.Schlessinger, B.Pezeshki, C.M.Ho, A.Sali, C.M.Westhoff, R.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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20927037 C.A.Wagner, O.Devuyst, H.Belge, S.Bourgeois, and P.Houillier (2011).
The rhesus protein RhCG: a new perspective in ammonium transport and distal urinary acidification.
  Kidney Int, 79, 154-161.  
21175663 N.M.Burton, and G.Daniels (2011).
Structural modelling of red cell surface proteins.
  Vox Sang, 100, 129-139.  
21455271 N.M.Burton, and L.J.Bruce (2011).
Modelling the structure of the red cell membrane.
  Biochem Cell Biol, 89, 200-215.  
21368153 U.Akgun, and S.Khademi (2011).
Periplasmic vestibule plays an important role for solute recruitment, selectivity, and gating in the Rh/Amt/MEP superfamily.
  Proc Natl Acad Sci U S A, 108, 3970-3975.  
20739007 J.K.Lee, and R.M.Stroud (2010).
Unlocking the eukaryotic membrane protein structural proteome.
  Curr Opin Struct Biol, 20, 464-470.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.