7NRN

NMR structure of GIPC1-GH2 domain

7NRN の概要

• エントリーDOI: 10.2210/pdb7nrn/pdb
• NMR情報: BMRB: 34609
• 分子名称: PDZ domain-containing protein GIPC1 (1 entity in total)
• 機能のキーワード: alpha-helical bundle, protein binding, endocytosis
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9181.20

構造登録者

Barthe, P.,Roumestand, C. (登録日: 2021-03-04, 公開日: 2021-04-14, 最終更新日: 2024-06-19)

主引用文献

Dubois, C.,Planelles-Herrero, V.J.,Tillatte-Tripodi, C.,Delbecq, S.,Mammri, L.,Sirkia, E.M.,Ropars, V.,Roumestand, C.,Barthe, P.
Pressure and Chemical Unfolding of an alpha-Helical Bundle Protein: The GH2 Domain of the Protein Adaptor GIPC1.
Int J Mol Sci, 22:-, 2021

PubMed Abstract: When combined with NMR spectroscopy, high hydrostatic pressure is an alternative perturbation method used to destabilize globular proteins that has proven to be particularly well suited for exploring the unfolding energy landscape of small single-domain proteins. To date, investigations of the unfolding landscape of all-β or mixed-α/β protein scaffolds are well documented, whereas such data are lacking for all-α protein domains. Here we report the NMR study of the unfolding pathways of GIPC1-GH2, a small α-helical bundle domain made of four antiparallel α-helices. High-pressure perturbation was combined with NMR spectroscopy to unravel the unfolding landscape at three different temperatures. The results were compared to those obtained from classical chemical denaturation. Whatever the perturbation used, the loss of secondary and tertiary contacts within the protein scaffold is almost simultaneous. The unfolding transition appeared very cooperative when using high pressure at high temperature, as was the case for chemical denaturation, whereas it was found more progressive at low temperature, suggesting the existence of a complex folding pathway.

PubMed: 33808390
DOI: 10.3390/ijms22073597

実験手法

SOLUTION NMR