7QTS

GB1 in mammalian cells, 10 uM

7QTS の概要

• エントリーDOI: 10.2210/pdb7qts/pdb
• NMR情報: BMRB: 34701
• 分子名称: Immunoglobulin G-binding protein G (1 entity in total)
• 機能のキーワード: gb1, b1 domain of streptococcal protein g, in-cell nmr, immune system
• 由来する生物種: Streptococcus sp.
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6360.00

構造登録者

Gerez, J.A.,Prymaczok, N.C.,Kadavath, H.,Gosh, D.,Butikofer, M.,Guntert, P.,Riek, R. (登録日: 2022-01-15, 公開日: 2022-12-21, 最終更新日: 2024-06-19)

主引用文献

Gerez, J.A.,Prymaczok, N.C.,Kadavath, H.,Ghosh, D.,Butikofer, M.,Fleischmann, Y.,Guntert, P.,Riek, R.
Protein structure determination in human cells by in-cell NMR and a reporter system to optimize protein delivery or transexpression.
Commun Biol, 5:1322-1322, 2022

PubMed Abstract: Most experimental methods for structural biology proceed in vitro and therefore the contribution of the intracellular environment on protein structure and dynamics is absent. Studying proteins at atomic resolution in living mammalian cells has been elusive due to the lack of methodologies. In-cell nuclear magnetic resonance spectroscopy (in-cell NMR) is an emerging technique with the power to do so. Here, we improved current methods of in-cell NMR by the development of a reporter system that allows monitoring the delivery of exogenous proteins into mammalian cells, a process that we called here "transexpression". The reporter system was used to develop an efficient protocol for in-cell NMR which enables spectral acquisition with higher quality for both disordered and folded proteins. With this method, the 3D atomic resolution structure of the model protein GB1 in human cells was determined with a backbone root-mean-square deviation (RMSD) of 1.1 Å.

PubMed: 36460747
DOI: 10.1038/s42003-022-04251-6

実験手法

SOLUTION NMR