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| | ==Crystal Structure of the Human Rhesus Glycoprotein RhCG== | | ==Crystal Structure of the Human Rhesus Glycoprotein RhCG== |
| - | <StructureSection load='3hd6' size='340' side='right' caption='[[3hd6]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='3hd6' size='340' side='right'caption='[[3hd6]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3hd6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HD6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HD6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3hd6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HD6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HD6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bhs|3bhs]], [[3b9z|3b9z]], [[3b9w|3b9w]], [[2ns1|2ns1]], [[1u7g|1u7g]], [[2b2h|2b2h]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C15orf6, CDRC2, PDRC2, RHCG, RHGK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hd6 OCA], [https://pdbe.org/3hd6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hd6 RCSB], [https://www.ebi.ac.uk/pdbsum/3hd6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hd6 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3hd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hd6 OCA], [http://pdbe.org/3hd6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hd6 RCSB], [http://www.ebi.ac.uk/pdbsum/3hd6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hd6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RHCG_HUMAN RHCG_HUMAN]] Functions as an electroneutral and bidirectional ammonium transporter. May regulate transepithelial ammonia secretion.<ref>PMID:11062476</ref> <ref>PMID:14761968</ref> <ref>PMID:15929723</ref> <ref>PMID:16477434</ref> | + | [https://www.uniprot.org/uniprot/RHCG_HUMAN RHCG_HUMAN] Functions as an electroneutral and bidirectional ammonium transporter. May regulate transepithelial ammonia secretion.<ref>PMID:11062476</ref> <ref>PMID:14761968</ref> <ref>PMID:15929723</ref> <ref>PMID:16477434</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: CSMP, Center for Structures of Membrane Proteins]] | + | [[Category: Large Structures]] |
| - | [[Category: Chaudhary, S]] | + | [[Category: Chaudhary S]] |
| - | [[Category: Gruswitz, F]] | + | [[Category: Gruswitz F]] |
| - | [[Category: Ho, C M]] | + | [[Category: Ho C-M]] |
| - | [[Category: Ho, J D]] | + | [[Category: Ho JD]] |
| - | [[Category: Pezeshki, B]] | + | [[Category: Pezeshki B]] |
| - | [[Category: Stroud, R M]] | + | [[Category: Stroud RM]] |
| - | [[Category: Ammonia]]
| + | |
| - | [[Category: Ammonia transport]]
| + | |
| - | [[Category: Cell membrane]]
| + | |
| - | [[Category: Center for structures of membrane protein]]
| + | |
| - | [[Category: Channel]]
| + | |
| - | [[Category: Csmp]]
| + | |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Rhesus]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: Transport]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| - | [[Category: Transporter]]
| + | |
| Structural highlights
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.
References
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
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