1YP8

Solution structure of the cyclotide tricyclon A

1YP8 の概要

• エントリーDOI: 10.2210/pdb1yp8/pdb
• 分子名称: tricyclon A (1 entity in total)
• 機能のキーワード: beta-sheet, cystine knot, cyclic backbone, cyclotide, cell cycle
• 由来する生物種: Viola tricolor
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3506.96

構造登録者

Mulvenna, J.P.,Sando, L.,Craik, D.J. (登録日: 2005-01-30, 公開日: 2005-05-24, 最終更新日: 2024-10-09)

主引用文献

Mulvenna, J.P.,Sando, L.,Craik, D.J.
Processing of a 22 kDa precursor protein to produce the circular protein tricyclon A.
Structure, 13:691-701, 2005

PubMed Abstract: Cyclotides are a family of plant proteins that have the unusual combination of head-to-tail backbone cyclization and a cystine knot motif. They are exceptionally stable and show resistance to most chemical, physical, and enzymatic treatments. The structure of tricyclon A, a previously unreported cyclotide, is described here. In this structure, a loop that is disordered in other cyclotides forms a beta sheet that protrudes from the globular core. This study indicates that the cyclotide fold is amenable to the introduction of a range of structural elements without affecting the cystine knot core of the protein, which is essential for the stability of the cyclotides. Tricyclon A does not possess a hydrophobic patch, typical of other cyclotides, and has minimal hemolytic activity, making it suitable for pharmaceutical applications. The 22 kDa precursor protein of tricyclon A was identified and provides clues to the processing of these fascinating miniproteins.

PubMed: 15893660
DOI: 10.1016/j.str.2005.02.013

実験手法

SOLUTION NMR