5xjm
From Proteopedia
(Difference between revisions)
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<StructureSection load='5xjm' size='340' side='right' caption='[[5xjm]], [[Resolution|resolution]] 3.20Å' scene=''> | <StructureSection load='5xjm' size='340' side='right' caption='[[5xjm]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5xjm]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XJM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XJM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5xjm]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895], [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XJM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XJM FirstGlance]. <br> |
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAR:SARCOSINE'>SAR</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAR:SARCOSINE'>SAR</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5xli|5xli]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5xli|5xli]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AGTR2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=5xjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xjm OCA], [http://pdbe.org/5xjm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xjm RCSB], [http://www.ebi.ac.uk/pdbsum/5xjm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xjm 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=5xjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xjm OCA], [http://pdbe.org/5xjm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xjm RCSB], [http://www.ebi.ac.uk/pdbsum/5xjm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xjm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/AGTR2_HUMAN AGTR2_HUMAN]] Receptor for angiotensin II. Cooperates with MTUS1 to inhibit ERK2 activation and cell proliferation.<ref>PMID:15123706</ref> | [[http://www.uniprot.org/uniprot/AGTR2_HUMAN AGTR2_HUMAN]] Receptor for angiotensin II. Cooperates with MTUS1 to inhibit ERK2 activation and cell proliferation.<ref>PMID:15123706</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Angiotensin II (AngII) plays a central role in regulating human blood pressure, which is mainly mediated by interactions between AngII and the G-protein-coupled receptors (GPCRs) AngII type 1 receptor (AT1R) and AngII type 2 receptor (AT2R). We have solved the crystal structure of human AT2R binding the peptide ligand [Sar(1), Ile(8)]AngII and its specific antibody at 3.2-A resolution. [Sar(1), Ile(8)]AngII interacts with both the 'core' binding domain, where the small-molecule ligands of AT1R and AT2R bind, and the 'extended' binding domain, which is equivalent to the allosteric modulator binding site of muscarinic acetylcholine receptor. We generated an antibody fragment to stabilize the extended binding domain that functions as a positive allosteric modulator. We also identified a signature positively charged cluster, which is conserved among peptide-binding receptors, to locate C termini at the bottom of the binding pocket. The reported results should help with designing ligands for angiotensin receptors and possibly to other peptide GPCRs. | ||
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| + | Crystal structure of the human angiotensin II type 2 receptor bound to an angiotensin II analog.,Asada H, Horita S, Hirata K, Shiroishi M, Shiimura Y, Iwanari H, Hamakubo T, Shimamura T, Nomura N, Kusano-Arai O, Uemura T, Suno C, Kobayashi T, Iwata S Nat Struct Mol Biol. 2018 Jul;25(7):570-576. doi: 10.1038/s41594-018-0079-8. Epub, 2018 Jul 2. PMID:29967536<ref>PMID:29967536</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5xjm" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bacillus coli migula 1895]] | ||
| + | [[Category: Lk3 transgenic mice]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Asada, H]] | [[Category: Asada, H]] | ||
Revision as of 09:35, 18 July 2018
Complex structure of angiotensin II type 2 receptor with Fab
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