8B1X

Solution NMR structure of the single alpha helix peptide (P3-7)2

8B1X の概要

• エントリーDOI: 10.2210/pdb8b1x/pdb
• NMR情報: BMRB: 51591
• 分子名称: P3-7_2 (1 entity in total)
• 機能のキーワード: peptide design, single alpha helix, de novo protein
• 由来する生物種: unidentified
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2544.00

構造登録者

Escobedo, A.,Coles, M.,Diercks, T.,Garcia, J.,Millet, O.,Salvatella, X. (登録日: 2022-09-12, 公開日: 2023-01-25, 最終更新日: 2024-06-19)

主引用文献

Escobedo, A.,Piccirillo, J.,Aranda, J.,Diercks, T.,Mateos, B.,Garcia-Cabau, C.,Sanchez-Navarro, M.,Topal, B.,Biesaga, M.,Staby, L.,Kragelund, B.B.,Garcia, J.,Millet, O.,Orozco, M.,Coles, M.,Crehuet, R.,Salvatella, X.
A glutamine-based single alpha-helix scaffold to target globular proteins.
Nat Commun, 13:7073-7073, 2022

PubMed Abstract: The binding of intrinsically disordered proteins to globular ones can require the folding of motifs into α-helices. These interactions offer opportunities for therapeutic intervention but their modulation with small molecules is challenging because they bury large surfaces. Linear peptides that display the residues that are key for binding can be targeted to globular proteins when they form stable helices, which in most cases requires their chemical modification. Here we present rules to design peptides that fold into single α-helices by instead concatenating glutamine side chain to main chain hydrogen bonds recently discovered in polyglutamine helices. The resulting peptides are uncharged, contain only natural amino acids, and their sequences can be optimized to interact with specific targets. Our results provide design rules to obtain single α-helices for a wide range of applications in protein engineering and drug design.

PubMed: 36400768
DOI: 10.1038/s41467-022-34793-6

実験手法

SOLUTION NMR