6ln2

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<StructureSection load='6ln2' size='340' side='right'caption='[[6ln2]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='6ln2' size='340' side='right'caption='[[6ln2]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6ln2]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LN2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6LN2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6ln2]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pasteurianus"_(winogradsky_1895)_lehmann_and_neumann_1907 "bacillus pasteurianus" (winogradsky 1895) lehmann and neumann 1907] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LN2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6LN2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=97Y:N-{4-[(R)-(3,3-DIMETHYLCYCLOBUTYL)({6-[4-(TRIFLUOROMETHYL)-1H-IMIDAZOL-1-YL]PYRIDIN-3-YL}AMINO)METHYL]BENZENE-1-CARBONYL}-BETA-ALANINE'>97Y</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=97Y:N-{4-[(R)-(3,3-DIMETHYLCYCLOBUTYL)({6-[4-(TRIFLUOROMETHYL)-1H-IMIDAZOL-1-YL]PYRIDIN-3-YL}AMINO)METHYL]BENZENE-1-CARBONYL}-BETA-ALANINE'>97Y</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GLP1R ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1501 "Bacillus pasteurianus" (Winogradsky 1895) Lehmann and Neumann 1907])</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=6ln2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ln2 OCA], [http://pdbe.org/6ln2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ln2 RCSB], [http://www.ebi.ac.uk/pdbsum/6ln2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ln2 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=6ln2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ln2 OCA], [http://pdbe.org/6ln2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ln2 RCSB], [http://www.ebi.ac.uk/pdbsum/6ln2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ln2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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.
[[http://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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Glucagon-like peptide-1 receptor (GLP-1R) is a class B G protein-coupled receptor that plays an important role in glucose homeostasis and treatment of type 2 diabetes. Structures of full-length class B receptors were determined in complex with their orthosteric agonist peptides, however, little is known about their extracellular domain (ECD) conformations in the absence of orthosteric ligands, which has limited our understanding of their activation mechanism. Here, we report the 3.2 A resolution, peptide-free crystal structure of the full-length human GLP-1R in an inactive state, which reveals a unique closed conformation of the ECD. Disulfide cross-linking validates the physiological relevance of the closed conformation, while electron microscopy (EM) and molecular dynamic (MD) simulations suggest a large degree of conformational dynamics of ECD that is necessary for binding GLP-1. Our inactive structure represents a snapshot of the peptide-free GLP-1R and provides insights into the activation pathway of this receptor family.
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Full-length human GLP-1 receptor structure without orthosteric ligands.,Wu F, Yang L, Hang K, Laursen M, Wu L, Han GW, Ren Q, Roed NK, Lin G, Hanson MA, Jiang H, Wang MW, Reedtz-Runge S, Song G, Stevens RC Nat Commun. 2020 Mar 9;11(1):1272. doi: 10.1038/s41467-020-14934-5. PMID:32152292<ref>PMID:32152292</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 6ln2" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lk3 transgenic mice]]
[[Category: Han, G W]]
[[Category: Han, G W]]
[[Category: Hang, K]]
[[Category: Hang, K]]

Revision as of 10:35, 27 March 2020

Crystal structure of full length human GLP1 receptor in complex with Fab fragment (Fab7F38)

PDB ID 6ln2

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