ArticleJournal of biomolecular NMR2011
Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP.
Article in Journal of biomolecular NMR, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Intrinsically Disordered Tardigrade Proteins Self-Assemble into Fibrous Gels in Response to Environmental Stress.Angewandte Chemie (International ed. in English) · 2022Article
- Differential Recognition Preferences of the Three Src Homology 3 (SH3) Domains from the Adaptor CD2-associated Protein (CD2AP) and Direct Association with Ras and Rab Interactor 3 (RIN3).The Journal of biological chemistry · 2015Article
- A 45-Amino-Acid Scaffold Mined from the PDB for High-Affinity Ligand Engineering.Chemistry & biology · 2015Article
- Capping protein regulators fine-tune actin assembly dynamics.Nature reviews. Molecular cell biology · 2014Review
- Inhibition of CIN85-mediated invasion by a novel SH3 domain binding motif in the lysyl oxidase propeptide.PloS one · 2013Article
- Distinct ubiquitin binding modes exhibited by SH3 domains: molecular determinants and functional implications.PloS one · 2013Article
- Epithelial junction formation requires confinement of Cdc42 activity by a novel SH3BP1 complex.The Journal of cell biology · 2012Article
- Multi-timescale conformational dynamics of the SH3 domain of CD2-associated protein using NMR spectroscopy and accelerated molecular dynamics.Angewandte Chemie (International ed. in English) · 2012Article
- Characterizing weak protein-protein complexes by NMR residual dipolar couplings.European biophysics journal : EBJ · 2011Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
CD2 associated protein (CD2AP) is an adaptor protein that plays an important role in cell to cell union needed for the kidney function. It contains three N-terminal SH3 domains that are able to interact among others with CD2, ALIX, c-Cbl and Ubiquitin. To understand the role of the individual SH3 domains of this adaptor protein we have performed a complete structural, thermodynamic and dynamic characterization of the separate domains using NMR and DSC. The energetic contributions to the stability and the backbone dynamics have been related to the structural features of each domain using the structure-based FoldX algorithm. We have found that the N-terminal SH3 domain of both adaptor proteins CD2AP and CIN85 are the most stable SH3 domains that have been studied until now. This high stability is driven by a more extensive network of intra-molecular interactions. We believe that this increased stabilization of N-terminal SH3 domains in adaptor proteins is crucial to maintain the necessary conformation to establish the proper interactions critical for the recruitment of their natural targets.
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