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1u34

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==3D NMR structure of the first extracellular domain of CRFR-2beta, a type B1 G-protein coupled receptor==
==3D NMR structure of the first extracellular domain of CRFR-2beta, a type B1 G-protein coupled receptor==
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<StructureSection load='1u34' size='340' side='right'caption='[[1u34]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='1u34' size='340' side='right'caption='[[1u34]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1u34]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U34 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U34 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1u34]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U34 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U34 FirstGlance]. <br>
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</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=1u34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u34 OCA], [https://pdbe.org/1u34 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u34 RCSB], [https://www.ebi.ac.uk/pdbsum/1u34 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u34 ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1u34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u34 OCA], [https://pdbe.org/1u34 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u34 RCSB], [https://www.ebi.ac.uk/pdbsum/1u34 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u34 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CRFR2_MOUSE CRFR2_MOUSE]] This is a receptor for corticotropin releasing factor. Shows high-affinity CRF binding. Also binds to urocortin I, II and III. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
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[https://www.uniprot.org/uniprot/CRFR2_MOUSE CRFR2_MOUSE] This is a receptor for corticotropin releasing factor. Shows high-affinity CRF binding. Also binds to urocortin I, II and III. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1u34 ConSurf].
</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=1u34 ConSurf].
<div style="clear:both"></div>
<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 corticotropin-releasing factor (CRF) ligand family has diverse effects on the CNS, including the modulation of the stress response. The ligands' effects are mediated by binding to CRF G protein-coupled receptors. We have determined the 3D NMR structure of the N-terminal extracellular domain (ECD1) of the mouse CRF receptor 2beta, which is the major ligand recognition domain, and identified its ligand binding site by chemical-shift perturbation experiments. The fold is identified as a short consensus repeat (SCR), a common protein interaction module. Mutagenesis reveals the integrity of the hormone-binding site in the full-length receptor. This study proposes that the ECD1 captures the C-terminal segment of the ligand, whose N terminus then penetrates into the transmembrane region of the receptor to initiate signaling. Key residues of SCR in the ECD1 are conserved in the G protein-coupled receptor subfamily, suggesting the SCR fold in all of the ECD1s of this subfamily.
 
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NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor.,Grace CR, Perrin MH, DiGruccio MR, Miller CL, Rivier JE, Vale WW, Riek R Proc Natl Acad Sci U S A. 2004 Aug 31;101(35):12836-41. Epub 2004 Aug 23. PMID:15326300<ref>PMID:15326300</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 1u34" 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]]
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[[Category: Mus musculus]]
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[[Category: DiGruccio, M R]]
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[[Category: DiGruccio MR]]
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[[Category: Grace, C R]]
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[[Category: Grace CR]]
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[[Category: Miller, C L]]
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[[Category: Miller CL]]
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[[Category: Perrin, M H]]
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[[Category: Perrin MH]]
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[[Category: Riek, R]]
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[[Category: Riek R]]
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[[Category: Rivier, J E]]
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[[Category: Rivier JE]]
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[[Category: Vale, W W]]
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[[Category: Vale WW]]
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[[Category: Beta sheets and loop]]
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[[Category: Signaling protein]]
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Current revision

3D NMR structure of the first extracellular domain of CRFR-2beta, a type B1 G-protein coupled receptor

PDB ID 1u34

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