2rmi
From Proteopedia
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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 Wed Jan 23 12:38:50 2008
Categories: Single protein | Cervini, L. | Gulyas, J. | Riek, R. | Rivier, J. | Royappa, G.C.R. | Astressin | Crf antagonist | Neuropeptide | Nmr | Urocortins | Urotensins
