2rmi

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(New page: 200px<br /><applet load="2rmi" size="350" color="white" frame="true" align="right" spinBox="true" caption="2rmi" /> '''3D NMR structure of astressin'''<br /> ==Ov...)
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[[Image:2rmi.gif|left|200px]]<br /><applet load="2rmi" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2rmi" />
 
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'''3D NMR structure of astressin'''<br />
 
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==Overview==
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==3D NMR structure of astressin==
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The C-terminally amidated CRF antagonist astressin binds to CRF-R1 or, CRF-R2 receptors with low nanomolar affinity while the corresponding, astressin-acid has &gt;100 times less affinity. To understand the role of the, amide group in binding, the conformations of astressin-amide and, astressin-acid were studied in DMSO using NMR techniques. The 3D NMR, structures show that the backbones of both analogs prefer an alpha-helical, conformation, with a small kink around Gln(26). However, astressin-amide, has a well-defined helical structure from Leu(27) to Ile(41) and a, conformation very similar to the bioactive conformation reported by our, group (Grace et al., Proc Natl Acad Sci USA 2007, 104, 4858-4863). In, contrast, astressin-acid has an irregular helical conformation from, Arg(35) onward, including a rearrangement of the side chains in that, region. This structural difference highlights the crucial role of the, C-terminal amidation for stabilization of astressin's bioactive, conformation.
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<StructureSection load='2rmi' size='340' side='right'caption='[[2rmi]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2rmi]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RMI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RMI FirstGlance]. <br>
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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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DPN:D-PHENYLALANINE'>DPN</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene></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=2rmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rmi OCA], [https://pdbe.org/2rmi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rmi RCSB], [https://www.ebi.ac.uk/pdbsum/2rmi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rmi ProSAT]</span></td></tr>
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</table>
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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/rm/2rmi_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=2rmi 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 C-terminally amidated CRF antagonist astressin binds to CRF-R1 or CRF-R2 receptors with low nanomolar affinity while the corresponding astressin-acid has &gt;100 times less affinity. To understand the role of the amide group in binding, the conformations of astressin-amide and astressin-acid were studied in DMSO using NMR techniques. The 3D NMR structures show that the backbones of both analogs prefer an alpha-helical conformation, with a small kink around Gln(26). However, astressin-amide has a well-defined helical structure from Leu(27) to Ile(41) and a conformation very similar to the bioactive conformation reported by our group (Grace et al., Proc Natl Acad Sci USA 2007, 104, 4858-4863). In contrast, astressin-acid has an irregular helical conformation from Arg(35) onward, including a rearrangement of the side chains in that region. This structural difference highlights the crucial role of the C-terminal amidation for stabilization of astressin's bioactive conformation.
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==About this Structure==
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Astressin-amide and astressin-acid are structurally different in dimethylsulfoxide.,Grace CR, Cervini L, Gulyas J, Rivier J, Riek R Biopolymers. 2007 Oct 5-15;87(2-3):196-205. PMID:17657708<ref>PMID:17657708</ref>
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2RMI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RMI OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Astressin-amide and astressin-acid are structurally different in dimethylsulfoxide., Grace CR, Cervini L, Gulyas J, Rivier J, Riek R, Biopolymers. 2007 Oct 5-15;87(2-3):196-205. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17657708 17657708]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 2rmi" style="background-color:#fffaf0;"></div>
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[[Category: Cervini, L.]]
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== References ==
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[[Category: Gulyas, J.]]
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<references/>
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[[Category: Riek, R.]]
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__TOC__
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[[Category: Rivier, J.]]
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</StructureSection>
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[[Category: Royappa, G.C.R.]]
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[[Category: Large Structures]]
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[[Category: astressin]]
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[[Category: Cervini L]]
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[[Category: crf antagonist]]
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[[Category: Gulyas J]]
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[[Category: neuropeptide]]
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[[Category: Riek R]]
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[[Category: nmr]]
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[[Category: Rivier J]]
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[[Category: urocortins]]
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[[Category: Royappa GCR]]
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[[Category: urotensins]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:38:50 2008''
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Current revision

3D NMR structure of astressin

PDB ID 2rmi

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