1VRZ

Helix turn helix motif

「1Q4F」から置き換えられました

1VRZ の概要

• エントリーDOI: 10.2210/pdb1vrz/pdb
• 分子名称: DE NOVO DESIGNED 21 RESIDUE PEPTIDE, ACETATE ION (3 entities in total)
• 機能のキーワード: hth, helix-turn-helix motif, de novo protein
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2200.41

構造登録者

Rudresh,Ramakumar, S.,Ramagopal, U.A.,Inai, Y.,Sahal, D. (登録日: 2005-10-14, 公開日: 2005-11-01, 最終更新日: 2023-12-27)

主引用文献

Rudresh,Ramakumar, S.,Ramagopal, U.A.,Inai, Y.,Goel, S.,Sahal, D.,Chauhan, V.S.
De Novo Design and Characterization of a Helical Hairpin Eicosapeptide; Emergence of an Anion Receptor in the Linker Region.
Structure, 12:389-396, 2004

PubMed Abstract: De novo design of supersecondary structures is expected to provide useful molecular frameworks for the incorporation of functional sites as in proteins. A 21 residue long, dehydrophenylalanine-containing peptide has been de novo designed and its crystal structure determined. The apolar peptide folds into a helical hairpin supersecondary structure with two right-handed helices, connected by a tetraglycine linker. The helices of the hairpin interact with each other through a combination of C-H.O and N-H.O hydrogen bonds. The folding of the apolar peptide has been realized without the help of either metal ions or disulphide bonds. A remarkable feature of the peptide is the unanticipated occurrence of an anion binding motif in the linker region, strikingly similar in conformation and function to the "nest" motif seen in several proteins. The observation supports the view for the possible emergence of rudimentary functions over short sequence stretches in the early peptides under prebiotic conditions.

PubMed: 15016355
DOI: 10.1016/j.str.2004.02.014

実験手法

X-RAY DIFFRACTION (1.05 Å)