5TPH

Crystal structure of a de novo designed protein homodimer with curved beta-sheet

5TPH の概要

• エントリーDOI: 10.2210/pdb5tph/pdb
• 関連するPDBエントリー: 5TPJ
• 分子名称: de novo NTF2 homodimer, DI(HYDROXYETHYL)ETHER, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: de novo ntf2, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28970.76

構造登録者

Basanta, B.,Marcos, E.,Oberdorfer, G.,Chidyausiku, T.M.,Sankaran, B.,Baker, D. (登録日: 2016-10-20, 公開日: 2017-01-25, 最終更新日: 2024-03-06)

主引用文献

Marcos, E.,Basanta, B.,Chidyausiku, T.M.,Tang, Y.,Oberdorfer, G.,Liu, G.,Swapna, G.V.,Guan, R.,Silva, D.A.,Dou, J.,Pereira, J.H.,Xiao, R.,Sankaran, B.,Zwart, P.H.,Montelione, G.T.,Baker, D.
Principles for designing proteins with cavities formed by curved beta sheets.
Science, 355:201-206, 2017

PubMed Abstract: Active sites and ligand-binding cavities in native proteins are often formed by curved β sheets, and the ability to control β-sheet curvature would allow design of binding proteins with cavities customized to specific ligands. Toward this end, we investigated the mechanisms controlling β-sheet curvature by studying the geometry of β sheets in naturally occurring protein structures and folding simulations. The principles emerging from this analysis were used to design, de novo, a series of proteins with curved β sheets topped with α helices. Nuclear magnetic resonance and crystal structures of the designs closely match the computational models, showing that β-sheet curvature can be controlled with atomic-level accuracy. Our approach enables the design of proteins with cavities and provides a route to custom design ligand-binding and catalytic sites.

PubMed: 28082595
DOI: 10.1126/science.aah7389

実験手法

X-RAY DIFFRACTION (2.47 Å)