ArticleScientific reports2019
Mapping the allosteric network within a SH3 domain.
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 17 papers.
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Who cites it
17 citing papers in PubMed, 24 citations in OpenAlex.
- Allosteric Protein Chemical Shift Perturbations are Ubiquitous.bioRxiv : the preprint server for biology · 2026Article
- Robust SH2 binding affinity indicates minimal SH3-to-SH2 communication in Grb2.Biology direct · 2026Article
- SH3 domains selectively activate the PI3 kinase through non-conventional tertiary contacts.Communications biology · 2026Article
- Allosteric modulation of Grb2 drives ligand-dependent signal responses.Biology direct · 2025Article
- GRB2: A dynamic adaptor protein orchestrating cellular signaling in health and disease.Biochemistry and biophysics reports · 2024Review
- Targeting Grb2 SH3 Domains with Affimer Proteins Provides Novel Insights into Ras Signalling Modulation.Biomolecules · 2024Article
- An intramolecular energetic network regulates ligand recognition in a SH2 domain.Protein science : a publication of the Protein Society · 2023Article
- Biophysical Characterization of the Binding Mechanism between the MATH Domain of SPOP and Its Physiological Partners.International journal of molecular sciences · 2023Article
- On the Effects of Disordered Tails, Supertertiary Structure and Quinary Interactions on the Folding and Function of Protein Domains.Biomolecules · 2022Review
- Allosteric regulation of GRB2 modulates RAS activation.Small GTPases · 2022Article
- Experimental Characterization of the Interaction between the N-Terminal SH3 Domain of Crkl and C3G.International journal of molecular sciences · 2021Article
- EvoProDom: evolutionary modeling of protein families by assessing translocations of protein domains.FEBS open bio · 2021Article
- Double Mutant Cycles as a Tool to Address Folding, Binding, and Allostery.International journal of molecular sciences · 2021Review
- Article
- Supertertiary protein structure affects an allosteric network.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Understanding the Mechanism of Recognition of Gab2 by the N-SH2 Domain of SHP2.Life (Basel, Switzerland) · 2020Article
- Demonstration of Binding Induced Structural Plasticity in a SH2 Domain.Frontiers in molecular biosciences · 2020Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SH3 domains are very abundant protein-protein interactions modules, involved in the regulation of several cellular processes. Whilst they have been associated to allosteric communication pathways between contiguous domains in multi-domain proteins, there is lack of information regarding the intra-domain allosteric cross-talk within the SH3 moiety. Here we scrutinize the presence of an allosteric network in the C-terminal SH3 domain of Grb2 protein, upon binding the Grb2-associated binding 2 protein. To explore allostery, we performed double mutant cycle analysis, a powerful quantitative approach based on mutagenesis in conjunction with kinetic experiments. Data reveal the presence of an unexpected allosteric sparse network that modulates the affinity between the SH3 domain and its physiological partner.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.