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3c59

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{{Seed}}
 
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[[Image:3c59.png|left|200px]]
 
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==Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain==
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The line below this paragraph, containing "STRUCTURE_3c59", creates the "Structure Box" on the page.
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<StructureSection load='3c59' size='340' side='right'caption='[[3c59]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3c59]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C59 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=10M:DECYL+4-O-ALPHA-D-GLUCOPYRANOSYL-1-THIO-BETA-D-GLUCOPYRANOSIDE'>10M</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_3c59| PDB=3c59 | SCENE= }}
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3c5t|3c5t]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Glucagon-like peptide-1 receptor(GLP1R) ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3c59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c59 OCA], [https://pdbe.org/3c59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c59 RCSB], [https://www.ebi.ac.uk/pdbsum/3c59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c59 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/GLP1R_HUMAN GLP1R_HUMAN]] This is a receptor for glucagon-like peptide 1. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. [[https://www.uniprot.org/uniprot/EXE4_HELSU EXE4_HELSU]] Venom protein that mimics the incretin hormone glucagon-like peptide 1 (GLP-1). It stimulates insulin synthesis and secretion, protects against beta-cell apoptosis in response to different insults, and promotes beta-cell proliferation. It also promotes satiety, reduces food intake, reduces fat deposition, reduces body weight and inhibits gastric emptying. Interacts with GLP-1 receptor (GLP1R). Induces hypotension that is mediated by relaxation of cardiac smooth muscle.<ref>PMID:8405712</ref> <ref>PMID:19837656</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c5/3c59_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3c59 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The glucagon-like peptide-1 receptor (GLP-1R) belongs to Family B1 of the seven-transmembrane G protein-coupled receptors, and its natural agonist ligand is the peptide hormone glucagon-like peptide-1 (GLP-1). GLP-1 is involved in glucose homeostasis, and activation of GLP-1R in the plasma membrane of pancreatic beta-cells potentiates glucose-dependent insulin secretion. The N-terminal extracellular domain (nGLP-1R) is an important ligand binding domain that binds GLP-1 and the homologous peptide Exendin-4 with differential affinity. Exendin-4 has a C-terminal extension of nine amino acid residues known as the "Trp cage", which is absent in GLP-1. The Trp cage was believed to interact with nGLP-1R and thereby explain the superior affinity of Exendin-4. However, the molecular details that govern ligand binding and specificity of nGLP-1R remain undefined. Here we report the crystal structure of human nGLP-1R in complex with the antagonist Exendin-4(9-39) solved by the multiwavelength anomalous dispersion method to 2.2A resolution. The structure reveals that Exendin-4(9-39) is an amphipathic alpha-helix forming both hydrophobic and hydrophilic interactions with nGLP-1R. The Trp cage of Exendin-4 is not involved in binding to nGLP-1R. The hydrophobic binding site of nGLP-1R is defined by discontinuous segments including primarily a well defined alpha-helix in the N terminus of nGLP-1R and a loop between two antiparallel beta-strands. The structure provides for the first time detailed molecular insight into ligand binding of the human GLP-1 receptor, an established target for treatment of type 2 diabetes.
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===Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain===
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Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain.,Runge S, Thogersen H, Madsen K, Lau J, Rudolph R J Biol Chem. 2008 Apr 25;283(17):11340-7. Epub 2008 Feb 20. PMID:18287102<ref>PMID:18287102</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3c59" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18287102}}, adds the Publication Abstract to the page
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*[[Glucagon-like peptide 1 receptor|Glucagon-like peptide 1 receptor]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18287102 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18287102}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Human]]
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3C59 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C59 OCA].
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[[Category: Large Structures]]
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[[Category: Runge, S]]
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==Reference==
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<ref group="xtra">PMID:18287102</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
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[[Category: Runge, S.]]
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[[Category: Amidation]]
[[Category: Amidation]]
[[Category: Cleavage on pair of basic residue]]
[[Category: Cleavage on pair of basic residue]]
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[[Category: Ligand-bound g protein-coupled receptor]]
[[Category: Ligand-bound g protein-coupled receptor]]
[[Category: Membrane]]
[[Category: Membrane]]
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[[Category: Pharmaceutical]]
 
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[[Category: Polymorphism]]
 
[[Category: Secreted]]
[[Category: Secreted]]
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[[Category: Signaling protein/signaling protein complex]]
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[[Category: Signaling protein-signaling protein complex]]
[[Category: Transducer]]
[[Category: Transducer]]
[[Category: Transmembrane]]
[[Category: Transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 15:23:38 2009''
 

Current revision

Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain

PDB ID 3c59

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