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2rmi

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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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<StructureSection load='2rmi' size='340' side='right'caption='[[2rmi]], [[NMR_Ensembles_of_Models | 20 NMR models]]' 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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DPN:D-PHENYLALANINE'>DPN</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene></td></tr>
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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;'>[[2rm9|2rm9]], [[2rmd|2rmd]], [[2rme|2rme]], [[2rmf|2rmf]], [[2rmg|2rmg]], [[2rmh|2rmh]]</div></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/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=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 ==
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.
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, G C.R]]
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[[Category: urotensins]]
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[[Category: Astressin]]
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[[Category: Crf antagonist]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:48:29 2008''
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[[Category: Neuropeptide]]
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[[Category: Urocortin]]
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[[Category: Urotensin]]

Current revision

3D NMR structure of astressin

PDB ID 2rmi

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