2r4s: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2r4s.jpg|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_2r4s", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
-{{STRUCTURE_2r4s|  PDB=2r4s  |  SCENE=  }}
-'''Crystal structure of the human beta2 adrenoceptor'''
+==Crystal structure of the human beta2 adrenoceptor==
+<StructureSection load='2r4s' size='340' side='right'caption='[[2r4s]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2r4s]] is a 3 chain structure with sequence from [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=2R4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R4S 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]] 3.4&#8491;</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=2r4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r4s OCA], [https://pdbe.org/2r4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r4s RCSB], [https://www.ebi.ac.uk/pdbsum/2r4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r4s 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.
+== 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/r4/2r4s_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=2r4s ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Structural analysis of G-protein-coupled receptors (GPCRs) for hormones and neurotransmitters has been hindered by their low natural abundance, inherent structural flexibility, and instability in detergent solutions. Here we report a structure of the human beta2 adrenoceptor (beta2AR), which was crystallized in a lipid environment when bound to an inverse agonist and in complex with a Fab that binds to the third intracellular loop. Diffraction data were obtained by high-brilliance microcrystallography and the structure determined at 3.4 A/3.7 A resolution. The cytoplasmic ends of the beta2AR transmembrane segments and the connecting loops are well resolved, whereas the extracellular regions of the beta2AR are not seen. The beta2AR structure differs from rhodopsin in having weaker interactions between the cytoplasmic ends of transmembrane (TM)3 and TM6, involving the conserved E/DRY sequences. These differences may be responsible for the relatively high basal activity and structural instability of the beta2AR, and contribute to the challenges in obtaining diffraction-quality crystals of non-rhodopsin GPCRs.
-==Overview==
+Crystal structure of the human beta2 adrenergic G-protein-coupled receptor.,Rasmussen SG, Choi HJ, Rosenbaum DM, Kobilka TS, Thian FS, Edwards PC, Burghammer M, Ratnala VR, Sanishvili R, Fischetti RF, Schertler GF, Weis WI, Kobilka BK Nature. 2007 Nov 15;450(7168):383-7. Epub 2007 Oct 21. PMID:17952055<ref>PMID:17952055</ref>
-Structural analysis of G-protein-coupled receptors (GPCRs) for hormones and neurotransmitters has been hindered by their low natural abundance, inherent structural flexibility, and instability in detergent solutions. Here we report a structure of the human beta2 adrenoceptor (beta2AR), which was crystallized in a lipid environment when bound to an inverse agonist and in complex with a Fab that binds to the third intracellular loop. Diffraction data were obtained by high-brilliance microcrystallography and the structure determined at 3.4 A/3.7 A resolution. The cytoplasmic ends of the beta2AR transmembrane segments and the connecting loops are well resolved, whereas the extracellular regions of the beta2AR are not seen. The beta2AR structure differs from rhodopsin in having weaker interactions between the cytoplasmic ends of transmembrane (TM)3 and TM6, involving the conserved E/DRY sequences. These differences may be responsible for the relatively high basal activity and structural instability of the beta2AR, and contribute to the challenges in obtaining diffraction-quality crystals of non-rhodopsin GPCRs.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-R4S is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=2R4S OCA].
+</div>
+<div class="pdbe-citations 2r4s" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Crystal structure of the human beta2 adrenergic G-protein-coupled receptor., Rasmussen SG, Choi HJ, Rosenbaum DM, Kobilka TS, Thian FS, Edwards PC, Burghammer M, Ratnala VR, Sanishvili R, Fischetti RF, Schertler GF, Weis WI, Kobilka BK, Nature. 2007 Nov 15;450(7168):383-7. Epub 2007 Oct 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17952055 17952055]
+*[[Adrenergic receptor 3D structures|Adrenergic receptor 3D structures]]
+*[[G protein-coupled receptor|G protein-coupled receptor]]
+*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Protein complex]]
+[[Category: Burghammer M]]
-[[Category: Burghammer, M.]]
+[[Category: Choi HJ]]
-[[Category: Choi, H J.]]
+[[Category: Edwards PC]]
-[[Category: Edwards, P C.]]
+[[Category: Fischetti RF]]
-[[Category: Fischetti, R F.]]
+[[Category: Kobilka BK]]
-[[Category: Kobilka, B K.]]
+[[Category: Kobilka TS]]
-[[Category: Kobilka, T S.]]
+[[Category: Rasmussen SGF]]
-[[Category: Rasmussen, S G.]]
+[[Category: Ratnala VR]]
-[[Category: Ratnala, V R.]]
+[[Category: Rosenbaum DM]]
-[[Category: Rosenbaum, D M.]]
+[[Category: Sanishvili R]]
-[[Category: Sanishvili, R.]]
+[[Category: Schertler GF]]
-[[Category: Schertler, G F.]]
+[[Category: Thian FS]]
-[[Category: Thian, F S.]]
+[[Category: Weis WI]]
-[[Category: Weis, W I.]]
-[[Category: G-protein coupled receptor]]
-[[Category: Glycoprotein]]
-[[Category: Lipoprotein]]
-[[Category: Palmitate]]
-[[Category: Phosphorylation]]
-[[Category: Polymorphism]]
-[[Category: Receptor]]
-[[Category: Signaling protein]]
-[[Category: Transducer]]
-[[Category: Transmembrane helix]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 16:14:12 2008''