2rmi: Difference between revisions

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[[Image:2rmi.gif|left|200px]]


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==3D NMR structure of astressin==
The line below this paragraph, containing "STRUCTURE_2rmi", creates the "Structure Box" on the page.
<StructureSection load='2rmi' size='340' side='right'caption='[[2rmi]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
{{STRUCTURE_2rmi| PDB=2rmi  | SCENE= }}
<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>
 
</table>
'''3D NMR structure of astressin'''
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
==Overview==
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rm/2rmi_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==About this Structure==
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>
2RMI is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RMI OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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://www.ncbi.nlm.nih.gov/pubmed/17657708 17657708]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 2rmi" style="background-color:#fffaf0;"></div>
[[Category: Cervini, L.]]
== References ==
[[Category: Gulyas, J.]]
<references/>
[[Category: Riek, R.]]
__TOC__
[[Category: Rivier, J.]]
</StructureSection>
[[Category: Royappa, G C.R.]]
[[Category: Large Structures]]
[[Category: Astressin]]
[[Category: Cervini L]]
[[Category: Crf antagonist]]
[[Category: Gulyas J]]
[[Category: Neuropeptide]]
[[Category: Riek R]]
[[Category: Nmr]]
[[Category: Rivier J]]
[[Category: Urocortin]]
[[Category: Royappa GCR]]
[[Category: Urotensin]]
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Retrieved from "https://proteopedia.org/2rmi"