5UBS

Solution NMR Structure of NERD-S, a natively folded pentamutant of the B1 domain of streptococcal protein G (GB1) with a solvent-exposed Trp43

5UBS の概要

• エントリーDOI: 10.2210/pdb5ubs/pdb
• 関連するPDBエントリー: 5UB0 5UCE 5UCF
• NMR情報: BMRB: 30221
• 分子名称: Immunoglobulin G-binding protein G (1 entity in total)
• 機能のキーワード: dynamics, computational design, conformational exchange, immunoglobulin-binding, de novo protein
• 由来する生物種: Streptococcus sp. GX7805
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6289.93

構造登録者

Damry, A.M.,Davey, J.A.,Goto, N.K.,Chica, R.A. (登録日: 2016-12-21, 公開日: 2017-08-23, 最終更新日: 2024-05-15)

主引用文献

Davey, J.A.,Damry, A.M.,Goto, N.K.,Chica, R.A.
Rational design of proteins that exchange on functional timescales.
Nat. Chem. Biol., 13:1280-1285, 2017

PubMed Abstract: Proteins are intrinsically dynamic molecules that can exchange between multiple conformational states, enabling them to carry out complex molecular processes with extreme precision and efficiency. Attempts to design novel proteins with tailored functions have mostly failed to yield efficiencies matching those found in nature because standard methods do not allow the design of exchange between necessary conformational states on a functionally relevant timescale. Here we developed a broadly applicable computational method to engineer protein dynamics that we term meta-multistate design. We used this methodology to design spontaneous exchange between two novel conformations introduced into the global fold of Streptococcal protein G domain β1. The designed proteins, named DANCERs, for dynamic and native conformational exchangers, are stably folded and switch between predicted conformational states on the millisecond timescale. The successful introduction of defined dynamics on functional timescales opens the door to new applications requiring a protein to spontaneously access multiple conformational states.

PubMed: 29058725
DOI: 10.1038/nchembio.2503

実験手法

SOLUTION NMR