2LAQ

Solution structure of the Sex Peptide from Drosophila melanogaster

2LAQ の概要

• エントリーDOI: 10.2210/pdb2laq/pdb
• NMR情報: BMRB: 17533
• 分子名称: Accessory gland-specific peptide 70A (1 entity in total)
• 機能のキーワード: hydroxiproline rich, signaling protein
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• 細胞内の位置: Secreted: P05623
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4435.04

構造登録者

Moehle, K.,Freund, A.,Robinson, J.A. (登録日: 2011-03-17, 公開日: 2011-04-27, 最終更新日: 2023-06-14)

主引用文献

Moehle, K.,Freund, A.,Kubli, E.,Robinson, J.A.
NMR studies of the solution conformation of the sex peptide from Drosophila melanogaster.
Febs Lett., 585:1197-1202, 2011

PubMed Abstract: The insect sex peptide (SP) elicits a variety of biological responses upon transfer to the mated female. SP contains 36 amino acids, including a tryptophan-rich N-terminal region, a central region containing five hydroxyproline (Hyp) residues, and a C-terminal region enclosed by a disulfide bridge. The solution structure of SP, studied here using NMR spectroscopy, includes a motif WPWN that adopts a type I β-turn in the N-terminal Trp-rich region. This turn region is connected to the central Hyp-rich region, which adopts extended and/or PPII-like conformations. The C-terminal disulfide-bonded loop populates helical turns or nascent helical structure. Overall, the results reveal a rather flexible peptide that lacks a compact folded structure in solution.

PubMed: 21439282
DOI: 10.1016/j.febslet.2011.03.040

実験手法

SOLUTION NMR