7NRN

NMR structure of GIPC1-GH2 domain

Summary for 7NRN

• Entry DOI: 10.2210/pdb7nrn/pdb
• NMR Information: BMRB: 34609
• Descriptor: PDZ domain-containing protein GIPC1 (1 entity in total)
• Functional Keywords: alpha-helical bundle, protein binding, endocytosis
• Biological source: Mus musculus (Mouse)
• Total number of polymer chains: 1
• Total formula weight: 9181.20

Authors

Barthe, P.,Roumestand, C. (deposition date: 2021-03-04, release date: 2021-04-14, Last modification date: 2024-06-19)

Primary citation

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

Experimental method

SOLUTION NMR