2rmi
From Proteopedia
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| - | [[Image:2rmi.gif|left|200px]] | + | [[Image:2rmi.gif|left|200px]] |
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| - | '''3D NMR structure of astressin''' | + | {{Structure |
| + | |PDB= 2rmi |SIZE=350|CAPTION= <scene name='initialview01'>2rmi</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''3D NMR structure of astressin''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2RMI is a [ | + | 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]. |
==Reference== | ==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:[http:// | + | 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] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cervini, L.]] | [[Category: Cervini, L.]] | ||
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[[Category: neuropeptide]] | [[Category: neuropeptide]] | ||
[[Category: nmr]] | [[Category: nmr]] | ||
| - | [[Category: | + | [[Category: urocortin]] |
| - | [[Category: | + | [[Category: urotensin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:37:31 2008'' |
Revision as of 16:37, 20 March 2008
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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 of sequence from [1]. 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 Thu Mar 20 18:37:31 2008
Categories: Single protein | Cervini, L. | Gulyas, J. | Riek, R. | Rivier, J. | Royappa, G C.R. | Astressin | Crf antagonist | Neuropeptide | Nmr | Urocortin | Urotensin
