ArticleArchives of biochemistry and biophysics2007
Structural and energetic aspects of Grb2-SH2 domain-swapping.
Article in Archives of biochemistry and biophysics, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
- Structural basis of binding the unique N-terminal domain of microtubule-associated protein 2c to proteins regulating kinases of signaling pathways.The Journal of biological chemistry · 2024Article
- GRB2 dimerization mediated by SH2 domain-swapping is critical for T cell signaling and cytokine production.Scientific reports · 2023Article
- Synthesis and structural characterization of a monocarboxylic inhibitor for GRB2 SH2 domain.Bioorganic & medicinal chemistry letters · 2021Article
- Some thermodynamic effects of varying nonpolar surfaces in protein-ligand interactions.European journal of medicinal chemistry · 2020Article
- The dynamics of free and phosphopeptide-bound Grb2-SH2 reveals two dynamically independent subdomains and an encounter complex with fuzzy interactions.Scientific reports · 2020Article
- Small molecule AX-024 reduces T cell proliferation independently of CD3ϵ/Nck1 interaction, which is governed by a domain swap in the Nck1-SH3.1 domain.The Journal of biological chemistry · 2020Article
- Structural and functional properties of Grb2 SH2 dimer in CD28 binding.Biophysics and physicobiology · 2019Article
- Bridging the Gap: Modulatory Roles of the Grb2-Family Adaptor, Gads, in Cellular and Allergic Immune Responses.Frontiers in immunology · 2019Review
- Structural Determinants of Misfolding in Multidomain Proteins.PLoS computational biology · 2016Article
- Structural and biophysical investigation of the interaction of a mutant Grb2 SH2 domain (W121G) with its cognate phosphopeptide.Protein science : a publication of the Protein Society · 2016Article
- Structural insights into the intertwined dimer of fyn SH2.Protein science : a publication of the Protein Society · 2015Article
- Evaluation of the interaction between phosphohistidine analogues and phosphotyrosine binding domains.Chembiochem : a European journal of chemical biology · 2014Article
- Acidic pH promotes oligomerization and membrane insertion of the BclXL apoptotic repressor.Archives of biochemistry and biophysics · 2012Article
- Dimerization in the Grb7 protein.Journal of molecular recognition : JMR · 2012Article
- Functional repertoire, molecular pathways and diseases associated with 3D domain swapping in the human proteome.Journal of clinical bioinformatics · 2012Article
- Ligand binding and membrane insertion compete with oligomerization of the BclXL apoptotic repressor.Journal of molecular biology · 2012Article
- Limiting assumptions in structure-based design: binding entropy.Journal of computer-aided molecular design · 2012Review
- Protein-ligand interactions: thermodynamic effects associated with increasing nonpolar surface area.Journal of the American Chemical Society · 2011Article
- Binding of flexible and constrained ligands to the Grb2 SH2 domain: structural effects of ligand preorganization.Acta crystallographica. Section D, Biological crystallography · 2010Article
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
The SH2 domain of growth factor receptor-bound protein 2 (Grb2) has been the focus of numerous studies, primarily because of the important roles it plays in signal transduction. More recently, it has emerged as a useful protein to study the consequences of ligand preorganization upon energetics and structure in protein-ligand interactions. The Grb2-SH2 domain is known to form a domain-swapped dimer, and as part of our investigations toward correlating structure and energetics in biological systems, we examined the effects that domain-swapping dimerization of the Grb2-SH2 domain had upon ligand binding affinities. Isothermal titration calorimetry was performed using Grb2-SH2 in both its monomeric and domain-swapped dimeric forms and a phosphorylated tripeptide AcNH-pTyr-Val-Asn-NH(2) that is similar to the Shc sequence recognized by Grb2-SH2 in vivo. The two binding sites of domain-swapped dimer exhibited a 4- and a 13-fold reduction in ligand affinity compared to monomer. Crystal structures of peptide-bound and uncomplexed forms of Grb2-SH2 domain-swapped dimer were obtained and reveal that the orientation of residues V122, V123, and R142 may influence the conformation of W121, an amino acid that is believed to play an important role in Grb2-SH2 ligand sequence specificity. These findings suggest that domain-swapping of Grb2-SH2 not only results in a lower affinity for a Shc-derived ligand, but it may also affect ligand specificity.
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