|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Complex structure of angiotensin II type 2 receptor with Fab== | | ==Complex structure of angiotensin II type 2 receptor with Fab== |
| - | <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/"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> | + | <table><tr><td colspan='2'>[[5xjm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli], [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://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 [https://proteopedia.org/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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5xli|5xli]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAR:SARCOSINE'>SAR</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=5xjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xjm OCA], [https://pdbe.org/5xjm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xjm RCSB], [https://www.ebi.ac.uk/pdbsum/5xjm PDBsum], [https://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> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/AGTR2_HUMAN AGTR2_HUMAN]] X-linked non-syndromic intellectual disability. | + | [https://www.uniprot.org/uniprot/AGTR2_HUMAN AGTR2_HUMAN] X-linked non-syndromic intellectual disability. |
| | == 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> | + | [https://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX] Electron-transport protein of unknown function.[https://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 26: |
Line 25: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Homo sapiens]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Mus musculus]] | | [[Category: Mus musculus]] |
| - | [[Category: Asada, H]] | + | [[Category: Asada H]] |
| - | [[Category: Horita, S]] | + | [[Category: Horita S]] |
| - | [[Category: Iwata, S]] | + | [[Category: Iwata S]] |
| - | [[Category: Shimamura, T]] | + | [[Category: Shimamura T]] |
| - | [[Category: Angiotensin receptor]]
| + | |
| - | [[Category: Class a gpcr]]
| + | |
| - | [[Category: Regulate human blood pressure]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Disease
AGTR2_HUMAN X-linked non-syndromic intellectual disability.
Function
C562_ECOLX Electron-transport protein of unknown function.AGTR2_HUMAN Receptor for angiotensin II. Cooperates with MTUS1 to inhibit ERK2 activation and cell proliferation.[1]
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.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nouet S, Amzallag N, Li JM, Louis S, Seitz I, Cui TX, Alleaume AM, Di Benedetto M, Boden C, Masson M, Strosberg AD, Horiuchi M, Couraud PO, Nahmias C. Trans-inactivation of receptor tyrosine kinases by novel angiotensin II AT2 receptor-interacting protein, ATIP. J Biol Chem. 2004 Jul 9;279(28):28989-97. Epub 2004 Apr 29. PMID:15123706 doi:http://dx.doi.org/10.1074/jbc.M403880200
- ↑ 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. Crystal structure of the human angiotensin II type 2 receptor bound to an angiotensin II analog. Nat Struct Mol Biol. 2018 Jul;25(7):570-576. doi: 10.1038/s41594-018-0079-8. Epub, 2018 Jul 2. PMID:29967536 doi:http://dx.doi.org/10.1038/s41594-018-0079-8
|
