2rmi: Difference between revisions
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[[Image:2rmi.gif|left|200px]] | [[Image:2rmi.gif|left|200px]] | ||
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'''3D NMR structure of astressin''' | '''3D NMR structure of astressin''' | ||
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==About this Structure== | ==About this Structure== | ||
2RMI is a [[Single protein]] structure | 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.]] | ||
[[Category: | [[Category: Astressin]] | ||
[[Category: | [[Category: Crf antagonist]] | ||
[[Category: | [[Category: Neuropeptide]] | ||
[[Category: | [[Category: Nmr]] | ||
[[Category: | [[Category: Urocortin]] | ||
[[Category: | [[Category: Urotensin]] | ||
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Revision as of 14:10, 4 May 2008
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
