3UC7

Trp-cage cyclo-TC1 - monoclinic crystal form

3UC7 の概要

• エントリーDOI: 10.2210/pdb3uc7/pdb
• 関連するPDBエントリー: 2LL5 3UC8
• 分子名称: Cyclo-TC1, CHLORIDE ION (3 entities in total)
• 機能のキーワード: mini-protein, trp-cage, cyclic peptide, multimer, protein-protein interaction, de novo protein
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 12936.35

構造登録者

Scian, M.,Le Trong, I.,Stenkamp, R.E.,Andersen, N.H. (登録日: 2011-10-26, 公開日: 2012-07-18, 最終更新日: 2024-10-30)

主引用文献

Scian, M.,Lin, J.C.,Le Trong, I.,Makhatadze, G.I.,Stenkamp, R.E.,Andersen, N.H.
Crystal and NMR structures of a Trp-cage mini-protein benchmark for computational fold prediction.
Proc.Natl.Acad.Sci.USA, 109:12521-12525, 2012

PubMed Abstract: To provide high-resolution X-ray crystallographic structures of a peptide with the Trp-cage fold, we prepared a cyclized version of this motif. Cyclized Trp-cage is remarkably stable and afforded two crystal forms suitable for X-ray diffraction. The resulting higher resolution crystal structures validate the prior NMR models and provide explanations for experimental observations that could not be rationalized by NMR structural data, including the structural basis for the increase in fold stability associated with motif cyclization and the manner in which a polar serine side chain is accommodated in the hydrophobic interior. A hexameric oligomer of the cyclic peptide is found in both crystal forms and indicates that under appropriate conditions, this minimized system may also serve as a model for protein-protein interactions.

PubMed: 22802678
DOI: 10.1073/pnas.1121421109

実験手法

X-RAY DIFFRACTION (1.1 Å)