ArticleFEBS letters2012
Structural recognition mechanisms between human Src homology domain 3 (SH3) and ALG-2-interacting protein X (Alix).
Article in FEBS letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 9 citations in OpenAlex.
- Synergy and allostery in ligand binding by HIV-1 Nef.The Biochemical journal · 2021Article
- Effects and mechanisms of Eps8 on the biological behaviour of malignant tumours (Review).Oncology reports · 2021Review
- Atypical regulation of G protein-coupled receptor intracellular trafficking by ubiquitination.Current opinion in cell biology · 2014Review
- Developing advanced X-ray scattering methods combined with crystallography and computation.Methods (San Diego, Calif.) · 2013Review
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Authors and funding
13 authors at 7 institutions in 3 countries.
Funding
Abstract
The functions of Src family kinases are tightly regulated through Src homology (SH) domain-mediated protein-protein interactions. We previously reported the biophysical characteristics of the apoptosis-linked gene 2-interacting protein X (Alix) in complex with the haemopoietic cell kinase (Hck) SH3 domain. In the current study, we have combined ITC, NMR, SAXS and molecular modeling to determine a 3D model of the complex. We demonstrate that Hck SH3 recognizes an extended linear proline-rich region of Alix. This particular binding mode enables Hck SH3 to sense a specific non-canonical residue situated in the SH3 RT-loop of the kinase. The resulting model helps clarify the mechanistic insights of Alix-Hck interaction.
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