5f8u

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:42, 19 July 2023) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='5f8u' size='340' side='right'caption='[[5f8u]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
<StructureSection load='5f8u' size='340' side='right'caption='[[5f8u]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5f8u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Melga Melga]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F8U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F8U FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5f8u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F8U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F8U FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=P32:4-{[(2S)-3-(TERT-BUTYLAMINO)-2-HYDROXYPROPYL]OXY}-3H-INDOLE-2-CARBONITRILE'>P32</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]] 3.35&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4gpo|4gpo]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=P32:4-{[(2S)-3-(TERT-BUTYLAMINO)-2-HYDROXYPROPYL]OXY}-3H-INDOLE-2-CARBONITRILE'>P32</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADRB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9103 MELGA])</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=5f8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f8u OCA], [https://pdbe.org/5f8u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f8u RCSB], [https://www.ebi.ac.uk/pdbsum/5f8u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f8u 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=5f8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f8u OCA], [http://pdbe.org/5f8u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f8u RCSB], [http://www.ebi.ac.uk/pdbsum/5f8u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f8u ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/ADRB1_MELGA ADRB1_MELGA]] Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity.
+
[https://www.uniprot.org/uniprot/ADRB1_MELGA ADRB1_MELGA] Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity.
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
G protein-coupled receptors (GPCRs) mediate transmembrane signaling. Before ligand binding, GPCRs exist in a basal state. Crystal structures of several GPCRs bound with antagonists or agonists have been solved. However, the crystal structure of the ligand-free basal state of a GPCR, the starting point of GPCR activation and function, had not yet been determined. Here we report the X-ray crystal structure of the ligand-free basal state of a GPCR in a lipid membrane-like environment. Oligomeric turkey beta1-adrenergic receptors display two dimer interfaces. One interface involves the transmembrane domain (TM) 1, TM2, the C-terminal H8 and extracellular loop 1. The other interface engages residues from TM4, TM5, intracellular loop 2 and extracellular loop 2. Structural comparisons show that this ligand-free state is in an inactive conformation. This provides the structural basis of GPCR dimerization and oligomerization.
+
-
 
+
-
Crystal structure of oligomeric beta1-adrenergic G protein-coupled receptors in ligand-free basal state.,Huang J, Chen S, Zhang JJ, Huang XY Nat Struct Mol Biol. 2013 Apr;20(4):419-25. doi: 10.1038/nsmb.2504. Epub 2013 Feb, 24. PMID:23435379<ref>PMID:23435379</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 5f8u" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
*[[Adrenergic receptor 3D structures|Adrenergic receptor 3D structures]]
*[[Adrenergic receptor 3D structures|Adrenergic receptor 3D structures]]
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Melga]]
+
[[Category: Meleagris gallopavo]]
-
[[Category: Leslie, A G.W]]
+
[[Category: Leslie AGW]]
-
[[Category: Tate, C G]]
+
[[Category: Tate CG]]
-
[[Category: Warne, A]]
+
[[Category: Warne A]]
-
[[Category: Beta1-ar]]
+
-
[[Category: Cyanopindolol]]
+
-
[[Category: Signaling protein]]
+

Current revision

Ligand occupancy in crystal structure of beta1-adrenergic receptor previously submitted by Huang et al

PDB ID 5f8u

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5f8u"
Personal tools