2rh1
From Proteopedia
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- | [[Image:2rh1.png|left|200px]] | ||
- | + | ==High resolution crystal structure of human B2-adrenergic G protein-coupled receptor.== | |
+ | <StructureSection load='2rh1' size='340' side='right'caption='[[2rh1]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[2rh1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The April 2008 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Adrenergic Receptors'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2008_4 10.2210/rcsb_pdb/mom_2008_4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RH1 FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=12P:DODECAETHYLENE+GLYCOL'>12P</scene>, <scene name='pdbligand=ACM:ACETAMIDE'>ACM</scene>, <scene name='pdbligand=BU1:1,4-BUTANEDIOL'>BU1</scene>, <scene name='pdbligand=CAU:(2S)-1-(9H-CARBAZOL-4-YLOXY)-3-(ISOPROPYLAMINO)PROPAN-2-OL'>CAU</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2rh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rh1 OCA], [https://pdbe.org/2rh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rh1 RCSB], [https://www.ebi.ac.uk/pdbsum/2rh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rh1 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://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.[https://www.uniprot.org/uniprot/ENLYS_BPT4 ENLYS_BPT4] Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.<ref>PMID:22389108</ref> | ||
+ | == 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/rh/2rh1_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=2rh1 ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors constitute the largest family of eukaryotic signal transduction proteins that communicate across the membrane. We report the crystal structure of a human beta2-adrenergic receptor-T4 lysozyme fusion protein bound to the partial inverse agonist carazolol at 2.4 angstrom resolution. The structure provides a high-resolution view of a human G protein-coupled receptor bound to a diffusible ligand. Ligand-binding site accessibility is enabled by the second extracellular loop, which is held out of the binding cavity by a pair of closely spaced disulfide bridges and a short helical segment within the loop. Cholesterol, a necessary component for crystallization, mediates an intriguing parallel association of receptor molecules in the crystal lattice. Although the location of carazolol in the beta2-adrenergic receptor is very similar to that of retinal in rhodopsin, structural differences in the ligand-binding site and other regions highlight the challenges in using rhodopsin as a template model for this large receptor family. | ||
- | + | High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor.,Cherezov V, Rosenbaum DM, Hanson MA, Rasmussen SG, Thian FS, Kobilka TS, Choi HJ, Kuhn P, Weis WI, Kobilka BK, Stevens RC Science. 2007 Nov 23;318(5854):1258-65. Epub 2007 Oct 25. PMID:17962520<ref>PMID:17962520</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 2rh1" style="background-color:#fffaf0;"></div> | |
- | + | ||
==See Also== | ==See Also== | ||
*[[Adrenergic receptor|Adrenergic receptor]] | *[[Adrenergic receptor|Adrenergic receptor]] | ||
- | *[[ | + | *[[Adrenergic receptor 3D structures|Adrenergic receptor 3D structures]] |
- | + | *[[G protein-coupled receptor|G protein-coupled receptor]] | |
- | *[[ | + | *[[Lysozyme 3D structures|Lysozyme 3D structures]] |
- | *[[ | + | == References == |
- | + | <references/> | |
- | + | __TOC__ | |
- | == | + | </StructureSection> |
- | < | + | |
[[Category: Adrenergic Receptors]] | [[Category: Adrenergic Receptors]] | ||
- | [[Category: | + | [[Category: Escherichia virus T4]] |
+ | [[Category: Homo sapiens]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
- | + | [[Category: Cherezov V]] | |
- | [[Category: Cherezov | + | [[Category: Choi HJ]] |
- | [[Category: Choi | + | [[Category: Hanson MA]] |
- | + | [[Category: Kobilka BK]] | |
- | [[Category: Hanson | + | [[Category: Kobilka TS]] |
- | [[Category: Kobilka | + | [[Category: Kuhn P]] |
- | [[Category: Kobilka | + | [[Category: Rasmussen SGF]] |
- | [[Category: Kuhn | + | [[Category: Rosenbaum DM]] |
- | [[Category: Rasmussen | + | [[Category: Stevens RC]] |
- | [[Category: Rosenbaum | + | [[Category: Thian FS]] |
- | [[Category: Stevens | + | [[Category: Weis WI]] |
- | [[Category: Thian | + | |
- | [[Category: Weis | + | |
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Current revision
High resolution crystal structure of human B2-adrenergic G protein-coupled receptor.
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