1LE3

NMR Structure of Tryptophan Zipper 4: A Stable Beta-Hairpin Peptide Based on the C-terminal Hairpin of the B1 Domain of Protein G

「1HS0」から置き換えられました

1LE3 の概要

• エントリーDOI: 10.2210/pdb1le3/pdb
• 関連するPDBエントリー: 1LE0 1LE1
• 分子名称: Tryptophan Zipper 4 (1 entity in total)
• 機能のキーワード: beta-hairpin, type i beta-turn, protein binding
• 細胞内の位置: Secreted, cell wall; Peptidoglycan-anchor (Potential): P06654
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2012.09

構造登録者

Cochran, A.G.,Skelton, N.J.,Starovasnik, M.A. (登録日: 2002-04-09, 公開日: 2002-04-24, 最終更新日: 2024-10-09)

主引用文献

Cochran, A.G.,Skelton, N.J.,Starovasnik, M.A.
Tryptophan zippers: stable, monomeric beta -hairpins.
Proc.Natl.Acad.Sci.USA, 98:5578-5583, 2001

PubMed Abstract: A structural motif, the tryptophan zipper (trpzip), greatly stabilizes the beta-hairpin conformation in short peptides. Peptides (12 or 16 aa in length) with four different turn sequences are monomeric and fold cooperatively in water, as has been observed previously for some hairpin peptides. However, the folding free energies of the trpzips exceed substantially those of all previously reported beta-hairpins and even those of some larger designed proteins. NMR structures of three of the trpzip peptides reveal exceptionally well-defined beta-hairpin conformations stabilized by cross-strand pairs of indole rings. The trpzips are the smallest peptides to adopt an unique tertiary fold without requiring metal binding, unusual amino acids, or disulfide crosslinks.

PubMed: 11331745
DOI: 10.1073/pnas.091100898

実験手法

SOLUTION NMR