2l27

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[[Image:2l27.png|left|200px]]
 
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==NMR Structure of the ECD1 of CRF-R1 in complex with a peptide agonist==
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The line below this paragraph, containing "STRUCTURE_2l27", creates the "Structure Box" on the page.
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<StructureSection load='2l27' size='340' side='right'caption='[[2l27]]' 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'>[[2l27]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L27 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L27 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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, 20 models</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=2l27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l27 OCA], [https://pdbe.org/2l27 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l27 RCSB], [https://www.ebi.ac.uk/pdbsum/2l27 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l27 ProSAT]</span></td></tr>
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{{STRUCTURE_2l27| PDB=2l27 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CRFR1_HUMAN CRFR1_HUMAN] Receptor for corticotropin releasing factor (CRH). Shows high-affinity CRF binding. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.<ref>PMID:18801728</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/l2/2l27_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2l27 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 corticotropin-releasing factor (CRF) peptide hormone family members coordinate endocrine, behavioral, autonomic, and metabolic responses to stress and play important roles within the cardiovascular, gastrointestinal, and central nervous systems, among others. The actions of the peptides are mediated by activation of two G-protein-coupled receptors of the B1 family, CRF receptors 1 and 2 (CRF-R1 and CRF-R2alpha,beta). The recently reported three-dimensional structures of the first extracellular domain (ECD1) of both CRF-R1 and CRF-R2beta (Pioszak, A. A., Parker, N. R., Suino-Powell, K., and Xu, H. E. (2008) J. Biol. Chem. 283, 32900-32912; Grace, C. R., Perrin, M. H., Gulyas, J., Digruccio, M. R., Cantle, J. P., Rivier, J. E., Vale, W. W., and Riek, R. (2007) Proc. Natl. Acad. Sci. U.S.A. 104, 4858-4863) complexed with peptide antagonists provided a starting point in understanding the binding between CRF ligands and receptors at a molecular level. We now report the three-dimensional NMR structure of the ECD1 of human CRF-R1 complexed with a high affinity agonist, alpha-helical cyclic CRF. In the structure of the complex, the C-terminal residues (23-41) of alpha-helical cyclic CRF bind to the ECD1 of CRF-R1 in a helical conformation mainly along the hydrophobic face of the peptide in a manner similar to that of the antagonists in their corresponding ECD1 complex structures. Unique to this study is the observation that complex formation between an agonist and the ECD1-CRF-R1 promotes the helical conformation of the N terminus of the former, important for receptor activation (Gulyas, J., Rivier, C., Perrin, M., Koerber, S. C., Sutton, S., Corrigan, A., Lahrichi, S. L., Craig, A. G., Vale, W., and Rivier, J. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 10575-10579).
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===NMR Structure of the ECD1 of CRF-R1 in complex with a peptide agonist===
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NMR structure of the first extracellular domain of corticotropin-releasing factor receptor 1 (ECD1-CRF-R1) complexed with a high affinity agonist.,Grace CR, Perrin MH, Gulyas J, Rivier JE, Vale WW, Riek R J Biol Chem. 2010 Dec 3;285(49):38580-9. Epub 2010 Sep 15. PMID:20843795<ref>PMID:20843795</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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The line below this paragraph, {{ABSTRACT_PUBMED_20843795}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2l27" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20843795 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20843795}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[2l27]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L27 OCA].
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==Reference==
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<ref group="xtra">PMID:20843795</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Grace, C R.R.]]
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[[Category: Large Structures]]
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[[Category: Gulyas, J R.R.]]
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[[Category: Grace CRR]]
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[[Category: Perrin, M H.]]
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[[Category: Gulyas JRR]]
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[[Category: Riek, R R.]]
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[[Category: Perrin MH]]
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[[Category: Rivier, J E.]]
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[[Category: Riek RR]]
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[[Category: Vale, W W.]]
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[[Category: Rivier JE]]
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[[Category: Vale WW]]

Current revision

NMR Structure of the ECD1 of CRF-R1 in complex with a peptide agonist

PDB ID 2l27

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