3hd6
From Proteopedia
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| - | [[ | + | ==Crystal Structure of the Human Rhesus Glycoprotein RhCG== |
| + | <StructureSection load='3hd6' size='340' side='right' caption='[[3hd6]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3hd6]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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> | ||
| + | <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='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 Homo sapiens])</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://www.rcsb.org/pdb/explore.do?structureId=3hd6 RCSB], [http://www.ebi.ac.uk/pdbsum/3hd6 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hd/3hd6_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:20457942</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: CSMP, Center for Structures of Membrane Proteins | + | [[Category: CSMP, Center for Structures of Membrane Proteins]] |
| - | [[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, J D]] |
| - | [[Category: Pezeshki, B | + | [[Category: Pezeshki, B]] |
| - | [[Category: Stroud, R M | + | [[Category: Stroud, R M]] |
[[Category: Ammonia]] | [[Category: Ammonia]] | ||
[[Category: Ammonia transport]] | [[Category: Ammonia transport]] | ||
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[[Category: Membrane]] | [[Category: Membrane]] | ||
[[Category: Membrane protein]] | [[Category: Membrane protein]] | ||
| - | [[Category: Protein structure initiative | + | [[Category: PSI, Protein structure initiative]] |
| - | + | ||
[[Category: Rhesus]] | [[Category: Rhesus]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
Revision as of 09:28, 8 December 2014
Crystal Structure of the Human Rhesus Glycoprotein RhCG
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Categories: Homo sapiens | CSMP, Center for Structures of Membrane Proteins | Chaudhary, S | Gruswitz, F | Ho, C-.M | Ho, J D | Pezeshki, B | Stroud, R M | Ammonia | Ammonia transport | Cell membrane | Center for structures of membrane protein | Channel | Csmp | Glycoprotein | Membrane | Membrane protein | PSI, Protein structure initiative | Rhesus | Structural genomic | Transmembrane | Transport | Transport protein | Transporter
