ArticleScientific reports2019
The kinetics of folding of the NSH2 domain from p85.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 9 citations in OpenAlex.
- SH2 Domains: Folding, Binding and Therapeutical Approaches.International journal of molecular sciences · 2022Review
- Folding and Binding Mechanisms of the SH2 Domain from Crkl.Biomolecules · 2022Article
- Idelalisib activates AKT via increased recruitment of PI3Kδ/PI3Kβ to BCR signalosome while reducing PDK1 in post-therapy CLL cells.Leukemia · 2022Article
- Characterization of early and late transition states of the folding pathway of a SH2 domain.Protein science : a publication of the Protein Society · 2022Article
- Determining folding and binding properties of the C-terminal SH2 domain of SHP2.Protein science : a publication of the Protein Society · 2021Article
- A Quick Primer in Fluorescence-Based Equilibrium and Pre-steady State Methods for Determining Protein-Nucleotide Affinities.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Demonstration of Binding Induced Structural Plasticity in a SH2 Domain.Frontiers in molecular biosciences · 2020Article
- The Effect of ProlineInternational journal of molecular sciences · 2019Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SH2 domains are protein domains that mediate protein-protein interaction through the recognition and binding of specific sequences containing phosphorylated tyrosines. The p85 protein is the regulatory subunit of the heterodimeric enzyme PI3K, an important enzyme involved in several molecular pathways. In this work we characterize the folding kinetics of the NSH2 domain of p85. Our data clearly reveal peculiar folding kinetics, characterized by an apparent mismatch between the observed folding and unfolding kinetics. Taking advantage of double mixing stopped flow experiments and site directed mutagenesis we demonstrate that such behavior is due to the cis/trans isomerization of the peptide bond between D73 and P74, being in a cis conformation in the native protein. Our data are discussed in comparison with previous works on the folding of other SH2 domains.
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