2rmi

From Proteopedia

(Difference between revisions)

Current revision

3D NMR structure of astressin

Structural highlights

2rmi is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 20 models
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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 >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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Grace CR, Cervini L, Gulyas J, Rivier J, Riek R. Astressin-amide and astressin-acid are structurally different in dimethylsulfoxide. Biopolymers. 2007 Oct 5-15;87(2-3):196-205. PMID:17657708 doi:10.1002/bip.20818

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2rmi"

@@ Line 1: / Line 1: @@
 ==3D NMR structure of astressin==
-<StructureSection load='2rmi' size='340' side='right' caption='[[2rmi]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2rmi' size='340' side='right'caption='[[2rmi]]' scene=''>
 == Structural highlights ==
-<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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RMI FirstGlance]. <br>
+<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>
-</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>
+</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>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2rm9|2rm9]], [[2rmd|2rmd]], [[2rme|2rme]], [[2rmf|2rmf]], [[2rmg|2rmg]], [[2rmh|2rmh]]</td></tr>
+<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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rmi OCA], [http://pdbe.org/2rmi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rmi RCSB], [http://www.ebi.ac.uk/pdbsum/2rmi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rmi ProSAT]</span></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=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>
 == Evolutionary Conservation ==
@@ Line 13: / Line 13: @@
   <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/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 31: / Line 31: @@
 __TOC__
 </StructureSection>
-[[Category: Cervini, L]]
+[[Category: Large Structures]]
-[[Category: Gulyas, J]]
+[[Category: Cervini L]]
-[[Category: Riek, R]]
+[[Category: Gulyas J]]
-[[Category: Rivier, J]]
+[[Category: Riek R]]
-[[Category: Royappa, G C.R]]
+[[Category: Rivier J]]
-[[Category: Astressin]]
+[[Category: Royappa GCR]]
-[[Category: Crf antagonist]]
-[[Category: Neuropeptide]]
-[[Category: Urocortin]]
-[[Category: Urotensin]]

2rmi

From Proteopedia

Current revision

3D NMR structure of astressin

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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