2RMI
3D NMR structure of astressin
Summary for 2RMI
| Entry DOI | 10.2210/pdb2rmi/pdb |
| Related | 2rm9 2rmd 2rme 2rmf 2rmg 2rmh |
| Descriptor | astressin (1 entity in total) |
| Functional Keywords | crf antagonist, astressin, urocortins, urotensins, neuropeptide |
| Total number of polymer chains | 1 |
| Total formula weight | 3589.22 |
| Authors | Royappa, G.C.R.,Cervini, L.,Gulyas, J.,Rivier, J.,Riek, R. (deposition date: 2007-10-17, release date: 2007-10-30, Last modification date: 2024-11-20) |
| Primary citation | Grace, C.R.,Cervini, L.,Gulyas, J.,Rivier, J.,Riek, R. Astressin-amide and astressin-acid are structurally different in dimethylsulfoxide Biopolymers, 87:196-205, 2007 Cited by PubMed Abstract: 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. PubMed: 17657708DOI: 10.1002/bip.20818 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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