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2rmi

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[[Image:2rmi.gif|left|200px]]
[[Image:2rmi.gif|left|200px]]
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{{Structure
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|PDB= 2rmi |SIZE=350|CAPTION= <scene name='initialview01'>2rmi</scene>
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The line below this paragraph, containing "STRUCTURE_2rmi", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=DPN:D-PHENYLALANINE'>DPN</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene>
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{{STRUCTURE_2rmi| PDB=2rmi | SCENE= }}
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|RELATEDENTRY=[[2rm9|2rm9]], [[2rmd|2rmd]], [[2rme|2rme]], [[2rmf|2rmf]], [[2rmg|2rmg]], [[2rmh|2rmh]]
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|RESOURCES=<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://www.ebi.ac.uk/pdbsum/2rmi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2rmi RCSB]</span>
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'''3D NMR structure of astressin'''
'''3D NMR structure of astressin'''
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==About this Structure==
==About this Structure==
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2RMI is a [[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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2RMI is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RMI OCA].
==Reference==
==Reference==
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[[Category: Rivier, J.]]
[[Category: Rivier, J.]]
[[Category: Royappa, G C.R.]]
[[Category: Royappa, G C.R.]]
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[[Category: astressin]]
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[[Category: Astressin]]
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[[Category: crf antagonist]]
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[[Category: Crf antagonist]]
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[[Category: neuropeptide]]
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[[Category: Neuropeptide]]
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[[Category: nmr]]
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[[Category: Nmr]]
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[[Category: urocortin]]
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[[Category: Urocortin]]
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[[Category: urotensin]]
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[[Category: Urotensin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:10:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:02:00 2008''
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Revision as of 14:10, 4 May 2008

Template:STRUCTURE 2rmi

3D NMR structure of astressin


Overview

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.

About this Structure

2RMI is a Single protein structure. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sun May 4 17:10:34 2008

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