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6oba
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The beta2 adrenergic receptor bound to a negative allosteric modulator== |
| - | + | <StructureSection load='6oba' size='340' side='right'caption='[[6oba]], [[Resolution|resolution]] 3.10Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6oba]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OBA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OBA FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=JTZ:(2S)-1-[(1-METHYLETHYL)AMINO]-3-(2-PROP-2-EN-1-YLPHENOXY)PROPAN-2-OL'>JTZ</scene>, <scene name='pdbligand=M3J:6-bromo-N~2~-phenylquinazoline-2,4-diamine'>M3J</scene></td></tr> | |
| - | [[Category: | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr> |
| - | [[Category: | + | <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=6oba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oba OCA], [http://pdbe.org/6oba PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oba RCSB], [http://www.ebi.ac.uk/pdbsum/6oba PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oba ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ADRB2_HUMAN ADRB2_HUMAN]] Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Lysozyme]] | ||
| + | [[Category: ClarK, M]] | ||
| + | [[Category: Dengler, D]] | ||
| + | [[Category: Gmeiner, R]] | ||
| + | [[Category: Hirata, K]] | ||
[[Category: Hubner, H]] | [[Category: Hubner, H]] | ||
[[Category: Kaindl, J]] | [[Category: Kaindl, J]] | ||
| + | [[Category: Kobilka, B K]] | ||
[[Category: Korczynska, M]] | [[Category: Korczynska, M]] | ||
| - | [[Category: Gmeiner, R]] | ||
[[Category: Liu, X]] | [[Category: Liu, X]] | ||
| + | [[Category: Mahoney, J]] | ||
| + | [[Category: Matt, R A]] | ||
[[Category: Shoichet, B]] | [[Category: Shoichet, B]] | ||
| - | [[Category: Matt, R.A]] | ||
[[Category: Stanek, M]] | [[Category: Stanek, M]] | ||
[[Category: Stobel, A]] | [[Category: Stobel, A]] | ||
| - | [[Category: | + | [[Category: Sunahara, R]] |
| - | + | ||
[[Category: Xu, X]] | [[Category: Xu, X]] | ||
| - | [[Category: | + | [[Category: Allosteric modulator]] |
| - | [[Category: | + | [[Category: G protein coupled receptor]] |
| - | [[Category: | + | [[Category: Membrane protein]] |
| + | [[Category: Signal transduction]] | ||
| + | [[Category: Signaling protein]] | ||
Revision as of 10:10, 27 March 2020
The beta2 adrenergic receptor bound to a negative allosteric modulator
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Categories: Large Structures | Lysozyme | ClarK, M | Dengler, D | Gmeiner, R | Hirata, K | Hubner, H | Kaindl, J | Kobilka, B K | Korczynska, M | Liu, X | Mahoney, J | Matt, R A | Shoichet, B | Stanek, M | Stobel, A | Sunahara, R | Xu, X | Allosteric modulator | G protein coupled receptor | Membrane protein | Signal transduction | Signaling protein
