2RMI

3D NMR structure of astressin

2RMI の概要

• エントリーDOI: 10.2210/pdb2rmi/pdb
• 関連するPDBエントリー: 2rm9 2rmd 2rme 2rmf 2rmg 2rmh
• 分子名称: astressin (1 entity in total)
• 機能のキーワード: crf antagonist, astressin, urocortins, urotensins, neuropeptide
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3589.22

構造登録者

Royappa, G.C.R.,Cervini, L.,Gulyas, J.,Rivier, J.,Riek, R. (登録日: 2007-10-17, 公開日: 2007-10-30, 最終更新日: 2024-11-20)

主引用文献

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

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: 17657708
DOI: 10.1002/bip.20818

実験手法

SOLUTION NMR