3hd6

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Crystal Structure of the Human Rhesus Glycoprotein RhCG

Structural highlights

3hd6 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:BOG
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RHCG_HUMAN Functions as an electroneutral and bidirectional ammonium transporter. May regulate transepithelial ammonia secretion.[1] [2] [3] [4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Function of human Rh based on structure of RhCG at 2.1 A.,Gruswitz F, Chaudhary S, Ho JD, Schlessinger A, Pezeshki B, Ho CM, Sali A, Westhoff CM, Stroud RM Proc Natl Acad Sci U S A. 2010 May 25;107(21):9638-43. Epub 2010 May 10. PMID:20457942[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
30 reviews cite this structure
A Call for Systematic Research on Solute Carriers.
César-Razquin et al. (2015)
29 more
79 other articles
No citations found

References

  1. ↑ Marini AM, Matassi G, Raynal V, Andre B, Cartron JP, Cherif-Zahar B. The human Rhesus-associated RhAG protein and a kidney homologue promote ammonium transport in yeast. Nat Genet. 2000 Nov;26(3):341-4. PMID:11062476 doi:http://dx.doi.org/10.1038/81656
  2. ↑ Bakouh N, Benjelloun F, Hulin P, Brouillard F, Edelman A, Cherif-Zahar B, Planelles G. NH3 is involved in the NH4+ transport induced by the functional expression of the human Rh C glycoprotein. J Biol Chem. 2004 Apr 16;279(16):15975-83. Epub 2004 Feb 3. PMID:14761968 doi:http://dx.doi.org/10.1074/jbc.M308528200
  3. ↑ Zidi-Yahiaoui N, Mouro-Chanteloup I, D'Ambrosio AM, Lopez C, Gane P, Le van Kim C, Cartron JP, Colin Y, Ripoche P. Human Rhesus B and Rhesus C glycoproteins: properties of facilitated ammonium transport in recombinant kidney cells. Biochem J. 2005 Oct 1;391(Pt 1):33-40. PMID:15929723 doi:http://dx.doi.org/10.1042/BJ20050657
  4. ↑ Marini AM, Boeckstaens M, Benjelloun F, Cherif-Zahar B, Andre B. Structural involvement in substrate recognition of an essential aspartate residue conserved in Mep/Amt and Rh-type ammonium transporters. Curr Genet. 2006 Jun;49(6):364-74. Epub 2006 Feb 14. PMID:16477434 doi:http://dx.doi.org/10.1007/s00294-006-0062-5
  5. ↑ Gruswitz F, Chaudhary S, Ho JD, Schlessinger A, Pezeshki B, Ho CM, Sali A, Westhoff CM, Stroud RM. Function of human Rh based on structure of RhCG at 2.1 A. Proc Natl Acad Sci U S A. 2010 May 25;107(21):9638-43. Epub 2010 May 10. PMID:20457942

Contents


PDB ID 3hd6

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